1887
No metrics data to plot.
The attempt to load metrics for this article has failed.
The attempt to plot a graph for these metrics has failed.

EcoSal Plus

Domain 4:

Synthesis and Processing of Macromolecules

Nus Factors of

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.
  • Authors: Ranjan Sen1, Jisha Chalissery2, M. Zuhaib Qayyum3, V. Vishalini4, and Ghazala Muteeb5
  • Editor: Susan T. Lovett6
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Laboratory of Transcription Biology, Center for DNA Fingerprinting and Diagnostics, Nampally, Hyderabad 500001, India; 2: Laboratory of Transcription Biology, Center for DNA Fingerprinting and Diagnostics, Nampally, Hyderabad 500001, India; 3: Laboratory of Transcription Biology, Center for DNA Fingerprinting and Diagnostics, Nampally, Hyderabad 500001, India; 4: Laboratory of Transcription Biology, Center for DNA Fingerprinting and Diagnostics, Nampally, Hyderabad 500001, India; 5: Laboratory of Transcription Biology, Center for DNA Fingerprinting and Diagnostics, Nampally, Hyderabad 500001, India; 6: Department of Biology, Brandeis University, Waltham, MA
  • Received 08 July 2014 Accepted 10 October 2014 Published 21 November 2014
  • Address correspondence to Ranjan Sen, [email protected]
image of Nus Factors of <span class="jp-italic">Escherichia coli</span>
    Preview this reference work article:
    Preview Magnify
    Zoom in
    Zoomout

    Nus Factors of , Page 1 of 2

    | /docserver/preview/fulltext/ecosalplus/6/1/ESP-0008-2013-1.gif /docserver/preview/fulltext/ecosalplus/6/1/ESP-0008-2013-2.gif

  • Abstract:

    The highly conserved Nus factors of bacteria were discovered as essential host proteins for the growth of temperate phage λ in . Later, their essentiality and functions in transcription, translation, and, more recently, in DNA repair have been elucidated. Close involvement of these factors in various gene networks and circuits is also emerging from recent genomic studies. We have described a detailed overview of their biochemistry, structures, and various cellular functions, as well as their interactions with other macromolecules. Towards the end, we have envisaged different uncharted areas of studies with these factors, including their participation in pathogenicity.

  • Citation: Sen R, Chalissery J, Qayyum M, Vishalini V, Muteeb G. 2014. Nus Factors of , EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0008-2013

Article Version

This article is an updated version of the following content:
Nus Factors of

References

1. Friedman DI, Baron LS. 1974. Genetic characterization of a bacterial locus involved in the activity of the N function of phage lambda. Virology 58:141–148. [PubMed][CrossRef]
2. Friedman DI, Baumann M, Baron LS. 1976. Cooperative effects of bacterial mutations affecting lambda N gene expression. I. Isolation and characterization of a nusB mutant. Virology 73:119–127. [PubMed][CrossRef]
3. Romem M, Friedman CH. 1981. [Eye injuries and their prevention]. Harefuah 101:352–353. [PubMed]
4. Keppel F, Georgopoulos CP, Eisen H. 1974. Host interference with expression of the lambda N gene product. Biochimie 56:1505–1509. [PubMed][CrossRef]
5. Sullivan SL, Ward DF, Gottesman ME. 1992. Effect of Escherichia coli nusG function on lambda N-mediated transcription antitermination. J Bacteriol 174:1339–1344. [PubMed]
6. Zhou Y, Filter JJ, Court DL, Gottesman ME, Friedman DI. 2002. Requirement for NusG for transcription antitermination in vivo by the lambda N protein. J Bacteriol 184:3416–3418. [PubMed][CrossRef]
7. Greenblatt J, Li J, Adhya S, Friedman DI, Baron LS, Redfield B, Kung HF, Weissbach H. 1980. L factor that is required for beta-galactosidase synthesis is the nusA gene product involved in transcription termination. Proc Natl Acad Sci USA 77:1991–1994. [PubMed][CrossRef]
8. Greive SJ, Lins AF, von Hippel PH. 2005. Assembly of an RNA-protein complex. Binding of NusB and NusE (S10) proteins to boxA RNA nucleates the formation of the antitermination complex involved in controlling rRNA transcription in Escherichia coli. J Biol Chem 280:36397–36408. [PubMed][CrossRef]
9. Kung H, Spears C, Weissbach H. 1975. Purification and properties of a soluble factor required for the deoxyribonucleic acid-directed in vitro synthesis of beta-galactosidase. J Biol Chem 250:1556–1562. [PubMed]
10. Li J, Horwitz R, McCracken S, Greenblatt J. 1992. NusG, a new Escherichia coli elongation factor involved in transcriptional antitermination by the N protein of phage lambda. J Biol Chem 267:6012–6019. [PubMed]
11. Squires CL, Condon C, Seoh HK. 2003. Assay of antitermination of ribosomal RNA transcription. Methods Enzymol 371:472–487. [PubMed][CrossRef]
12. Swindle J, Zylicz M, Georgopoulos C, Li J, Greenblatt J. 1988. Purification and properties of the NusB protein of Escherichia coli. J Biol Chem 263:10229–10235. [PubMed]
13. Ciampi MS. 2006. Rho-dependent terminators and transcription termination. Microbiology 152(Pt 9) :2515–2528. [PubMed][CrossRef]
14. Squires CL, Zaporojets D. 2000. Proteins shared by the transcription and translation machines. Annu Rev Microbiol 54:775–798. [PubMed][CrossRef]
15. Downing WL, Sullivan SL, Gottesman ME, Dennis PP. 1990. Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon. J Bacteriol 172:1621–1627. [PubMed]
16. Rajapandi T, Oliver D. 1994. ssaD1, a suppressor of secA51(Ts) that renders growth of Escherichia coli cold sensitive, is an early amber mutation in the transcription factor gene nusB. J Bacteriol 176:4444–4447. [PubMed]
17. Zheng C, Friedman DI. 1994. Reduced Rho-dependent transcription termination permits NusA-independent growth of Escherichia coli. Proc Natl Acad Sci USA 91:7543–7547. [PubMed][CrossRef]
18. Bubunenko M, Baker T, Court DL. 2007. Essentiality of ribosomal and transcription antitermination proteins analyzed by systematic gene replacement in Escherichia coli. J Bacteriol 189:2844–2853. [PubMed][CrossRef]
19. Bylund GO, Lovgren JM, Wikstrom PM. 2001. Characterization of mutations in the metY-nusA-infB operon that suppress the slow growth of a DeltarimM mutant. J Bacteriol 183:6095–6106. [PubMed][CrossRef]
20. Greenblatt J, Li J. 1981. Interaction of the sigma factor and the nusA gene protein of E. coli with RNA polymerase in the initiation-termination cycle of transcription. Cell 24:421–428. [PubMed][CrossRef]
21. Greenblatt J, Li J. 1981. The nusA gene protein of Escherichia coli. Its identification and a demonstration that it interacts with the gene N transcription anti-termination protein of bacteriophage lambda. J Mol Biol 147:11–23. [PubMed][CrossRef]
22. Friedman DI, Olson ER. 1983. Evidence that a nucleotide sequence, “boxA,” is involved in the action of the NusA protein. Cell 34:143–149. [PubMed][CrossRef]
23. Olson ER, Flamm EL, Friedman DI. 1982. Analysis of nutR: a region of phage lambda required for antitermination of transcription. Cell 31:61–70. [PubMed][CrossRef]
24. Arnvig KB, Pennell S, Gopal B, Colston MJ. 2004. A high-affinity interaction between NusA and the rrn nut site in Mycobacterium tuberculosis. Proc Natl Acad Sci USA 101:8325–8330. [PubMed][CrossRef]
25. Cohen SE, Godoy VG, Walker GC. 2009. Transcriptional modulator NusA interacts with translesion DNA polymerases in Escherichia coli. J Bacteriol 191:665–672. [PubMed][CrossRef]
26. Borukhov S, Lee J, Laptenko O. 2005. Bacterial transcription elongation factors: new insights into molecular mechanism of action. Mol Microbiol 55:1315–1324. [PubMed][CrossRef]
27. Gibson TJ, Thompson JD, Heringa J. 1993. The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid. FEBS Lett 324:361–366. [PubMed][CrossRef]
28. Mah TF, Li J, Davidson AR, Greenblatt J. 1999. Functional importance of regions in Escherichia coli elongation factor NusA that interact with RNA polymerase, the bacteriophage lambda N protein and RNA. Mol Microbiol 34:523–537. [PubMed][CrossRef]
29. Worbs M, Bourenkov GP, Bartunik HD, Huber R, Wahl MC. 2001. An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. Mol Cell 7:1177–1189. [PubMed][CrossRef]
30. Liu K, Zhang Y, Severinov K, Das A, Hanna MM. 1996. Role of Escherichia coli RNA polymerase alpha subunit in modulation of pausing, termination and anti-termination by the transcription elongation factor NusA. EMBO J 15:150–161. [PubMed]
31. Schweimer K, Prasch S, Sujatha PS, Bubunenko M, Gottesman ME, Rosch P. 2011. NusA interaction with the alpha subunit of E. coli RNA polymerase is via the UP element site and releases autoinhibition. Structure 19:945–954. [PubMed][CrossRef]
32. Beuth B, Pennell S, Arnvig KB, Martin SR, Taylor IA. 2005. Structure of a Mycobacterium tuberculosis NusA-RNA complex. EMBO J 24:3576–3587. [PubMed][CrossRef]
33. Bonin I, Muhlberger R, Bourenkov GP, Huber R, Bacher A, Richter G, Wahl MC. 2004. Structural basis for the interaction of Escherichia coli NusA with protein N of phage lambda. Proc Natl Acad Sci USA 101:13762–13767. [PubMed][CrossRef]
34. Shin DH, Nguyen HH, Jancarik J, Yokota H, Kim R, Kim SH. 2003. Crystal structure of NusA from Thermotoga maritima and functional implication of the N-terminal domain. Biochemistry 42:13429–13437. [PubMed][CrossRef]
35. Gopal B, Haire LF, Gamblin SJ, Dodson EJ, Lane AN, Papavinasasundaram KG, Colston MJ, Dodson G. 2001. Crystal structure of the transcription elongation/anti-termination factor NusA from Mycobacterium tuberculosis at 1.7 Å resolution. J Mol Biol 314:1087–1095. [PubMed][CrossRef]
36. Eisenmann A, Schwarz S, Prasch S, Schweimer K, Rosch P. 2005. The E. coli NusA carboxy-terminal domains are structurally similar and show specific RNAP- and lambdaN interaction. Protein Sci 14:2018–2029. [PubMed][CrossRef]
37. Torres M, Condon C, Balada JM, Squires C, Squires CL. 2001. Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination. EMBO J 20:3811–3820. [PubMed][CrossRef]
38. Ghosh B, Das A. 1984. nusB: a protein factor necessary for transcription antitermination in vitro by phage lambda N gene product. Proc Natl Acad Sci USA 81:6305–6309. [PubMed][CrossRef]
39. Nodwell JR, Greenblatt J. 1993. Recognition of boxA antiterminator RNA by the E. coli antitermination factors NusB and ribosomal protein S10. Cell 72:261–268. [PubMed][CrossRef]
40. Squires CL, Greenblatt J, Li J, Condon C. 1993. Ribosomal RNA antitermination in vitro: requirement for Nus factors and one or more unidentified cellular components. Proc Natl Acad Sci USA 90:970–974. [PubMed][CrossRef]
41. Muhlberger R, Robelek R, Eisenreich W, Ettenhuber C, Sinner EK, Kessler H, Bacher A, Richter G. 2003. RNA DNA discrimination by the antitermination protein NusB. J Mol Biol 327:973–983. [PubMed][CrossRef]
42. Altieri AS, Mazzulla MJ, Horita DA, Coats RH, Wingfield PT, Das A, Court DL, Byrd RA. 2000. The structure of the transcriptional antiterminator NusB from Escherichia coli. Nat Struct Biol 7:470–474. [PubMed][CrossRef]
43. Huenges M, Rolz C, Gschwind R, Peteranderl R, Berglechner F, Richter G, Bacher A, Kessler H, Gemmecker G. 1998. Solution structure of the antitermination protein NusB of Escherichia coli: a novel all-helical fold for an RNA-binding protein. EMBO J 17:4092–4100. [PubMed][CrossRef]
44. Gopal B, Haire LF, Cox RA, Jo Colston M, Major S, Brannigan JA, Smerdon SJ, Dodson G. 2000. The crystal structure of NusB from Mycobacterium tuberculosis. Nat Struct Biol 7:475–478. [PubMed][CrossRef]
45. Bonin I, Robelek R, Benecke H, Urlaub H, Bacher A, Richter G,Wahl MC. 2004. Crystal structures of the antitermination factor NusB from Thermotoga maritima and implications for RNA binding. Biochem J 383(Pt 3) :419–428. [PubMed]
46. Noller HF, Nomura M. 1996. Ribosomes, p 167–186. In Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (ed), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd ed. ASM Press, Washington, DC.
47. Ohmori H, Friedberg EC, Fuchs RP, Goodman MF, Hanaoka F, Hinkle D, Kunkel TA, Lawrence CW, Livneh Z, Nohmi T, Prakash L, Prakash S, Todo T, Walker GC, Wang Z, Woodgate R. 2001. The Y-family of DNA polymerases. Mol Cell 8:7–8. [PubMed][CrossRef]
48. Gopal B, Papavinasasundaram KG, Dodson G, Colston MJ, Major SA, Lane AN. 2001. Spectroscopic and thermodynamic characterization of the transcription antitermination factor NusE and its interaction with NusB from Mycobacterium tuberculosis. Biochemistry 40:920–928. [PubMed][CrossRef]
49. Lüttgen H, Robelek R, Mühlberger R, Diercks T, Schuster SC, Köhler P, Kessler H, Bacher A, Richter G. 2002. Transcriptional regulation by antitermination. Interaction of RNA with NusB protein and NusB/NusE protein complex of Escherichia coli. J Mol Biol 316:875–885. [PubMed][CrossRef]
50. Brodersen DE, Clemons WM, Jr, Carter AP, Wimberly BT, Ramakrishnan V. 2002. Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 S RNA. J Mol Biol 316:725–768. [PubMed][CrossRef]
51. Burmann BM, Schweimer K, Luo X, Wahl MC, Stitt BL, Gottesman ME, Rösch P. 2010. A NusE:NusG complex links transcription and translation. Science 328:501–504. [PubMed][CrossRef]
52. Chalissery J, Muteeb G, Kalarickal NC, Mohan S, Jisha V, Sen R. 2011. Interaction surface of the transcription terminator Rho required to form a complex with the C-terminal domain of the antiterminator NusG. J Mol Biol 405:49–64. [PubMed][CrossRef]
53. Richardson JP. 2002. Rho-dependent termination and ATPases in transcript termination. Biochim Biophys Acta 1577:251–260. [PubMed][CrossRef]
54. Mooney RA, Schweimer K, Rosch P, Gottesman M, Landick R. 2009. Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators. J Mol Biol 391:341–358. [PubMed][CrossRef]
55. Drögemüller J, Stegmann CM, Mandal A, Steiner T, Burmann BM, Gottesman ME, Wöhrl BM, Rösch P, Wahl MC, Schweimer K. 2013. An autoinhibited state in the structure of Thermotoga maritima NusG. Structure 21:365–375. [PubMed][CrossRef]
56. Knowlton JR, Bubunenko M, Andrykovitch M, Guo W, Routzahn KM, Waugh DS, Court DL, Ji X. 2003. A spring-loaded state of NusG in its functional cycle is suggested by X-ray crystallography and supported by site-directed mutants. Biochemistry 42:2275–2281. [PubMed][CrossRef]
57. Steiner T, Kaiser JT, Marinkovic S, Huber R, Wahl MC. 2002. Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities. EMBO J 21:4641–4653. [PubMed][CrossRef]
58. Kyrpides NC, Woese CR, Ouzounis CA. 1996. KOW: a novel motif linking a bacterial transcription factor with ribosomal proteins. Trends Biochem Sci 21:425–426. [PubMed][CrossRef]
59. Wada T, Takagi T, Yamaguchi Y, Ferdous A, Imai T, Hirose S, Sugimoto S, Yano K, Hartzog GA, Winston F, Buratowski S, Handa H. 1998. DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs. Genes Dev 12:343–356. [PubMed][CrossRef]
60. Martinez-Rucobo FW, Sainsbury S, Cheung AC, Cramer P. 2011. Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity. EMBO J 30:1302–1310. [PubMed][CrossRef]
61. Klein BJ, Bose D, Baker KJ, Yusoff ZM, Zhang X, Murakami KS. 2011. RNA polymerase and transcription elongation factor Spt4/5 complex structure. Proc Natl Acad Sci USA 108:546–550. [PubMed][CrossRef]
62. Pasman Z, von Hippel PH. 2000. Regulation of rho-dependent transcription termination by NusG is specific to the Escherichia coli elongation complex. Biochemistry 39:5573–5585. [PubMed][CrossRef]
63. Reay P, Yamasaki K, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S. 2004. Structural and sequence comparisons arising from the solution structure of the transcription elongation factor NusG from Thermus thermophilus. Proteins 56:40–51. [PubMed][CrossRef]
64. Lawrence JG, Roth JR. 1996. Selfish operons: horizontal transfer may drive the evolution of gene clusters. Genetics 143:1843–1860. [PubMed]
65. Belogurov GA, Mooney RA, Svetlov V, Landick R, Artsimovitch I. 2009. Functional specialization of transcription elongation factors. EMBO J 28:112–122. [PubMed][CrossRef]
66. Burmann BM, Knauer SH, Sevostyanova A, Schweimer K, Mooney RA, Landick R, Artsimovitch I, Rösch P. 2012. An alpha helix to beta barrel domain switch transforms the transcription factor RfaH into a translation factor. Cell 150:291–303. [PubMed][CrossRef]
67. Belogurov GA, Vassylyeva MN, Svetlov V, Klyuyev S, Grishin NV, Vassylyev DG, Artsimovitch I. 2007. Structural basis for converting a general transcription factor into an operon-specific virulence regulator. Mol Cell 26:117–129. [PubMed][CrossRef]
68. Richardson JP, Greenblatt J. 1996. Control of RNA chain elongation and termination, p 822–848. In Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (ed), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd ed. ASM Press, Washington, DC.
69. Burns CM, Richardson LV, Richardson JP. 1998. Combinatorial effects of NusA and NusG on transcription elongation and Rho-dependent termination in Escherichia coli. J Mol Biol 278:307–316. [PubMed][CrossRef]
70. Burova E, Hung SC, Sagitov V, Stitt BL, Gottesman ME. 1995. Escherichia coli NusG protein stimulates transcription elongation rates in vivo and in vitro. J Bacteriol 177:1388–1392. [PubMed]
71. Artsimovitch I, Landick R. 2000. Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals. Proc Natl Acad Sci USA 97:7090–7095. [PubMed][CrossRef]
72. Kireeva ML, Kashlev M. 2009. Mechanism of sequence-specific pausing of bacterial RNA polymerase. Proc Natl Acad Sci USA 106:8900–8905. [PubMed][CrossRef]
73. Herbert KM, Greenleaf WJ, Block SM. 2008. Single-molecule studies of RNA polymerase: motoring along. Ann Rev Biochem 77:149–176. [PubMed][CrossRef]
74. Ha KS, Toulokhonov I, Vassylyev DG, Landick R. 2010. The NusA N-terminal domain is necessary and sufficient for enhancement of transcriptional pausing via interaction with the RNA exit channel of RNA polymerase. J Mol Biol 401:708–725. [PubMed][CrossRef]
75. Yang X, Molimau S, Doherty GP, Johnston EB, Marles-Wright J, Rothnagel R, Hankamer B, Lewis RJ, Lewis PJ. 2009. The structure of bacterial RNA polymerase in complex with the essential transcription elongation factor NusA. EMBO Rep 10:997–1002. [PubMed][CrossRef]
76. Bailey MJ, Hughes C, Koronakis V. 1996. Increased distal gene transcription by the elongation factor RfaH, a specialized homologue of NusG. Mol Microbiol 22:729–737. [PubMed][CrossRef]
77. Belogurov GA, Sevostyanova A, Svetlov V, Artsimovitch I. 2010. Functional regions of the N-terminal domain of the antiterminator RfaH. Mol Microbiol 76:286–301. [PubMed][CrossRef]
78. Sevostyanova A, Belogurov GA, Mooney RA, Landick R, Artsimovitch I. 2011. The beta subunit gate loop is required for RNA polymerase modification by RfaH and NusG. Mol Cell 43:253–262. [PubMed][CrossRef]
79. Artsimovitch I, Landick R. 2002. The transcriptional regulator RfaH stimulates RNA chain synthesis after recruitment to elongation complexes by the exposed nontemplate DNA strand. Cell 109:193–203. [PubMed][CrossRef]
80. Bailey MJ, Hughes C, Koronakis V. 2000. In vitro recruitment of the RfaH regulatory protein into a specialised transcription complex, directed by the nucleic acid ops element. Mol Gen Genet 262:1052–1059. [PubMed][CrossRef]
81. Svetlov V, Belogurov GA, Shabrova E, Vassylyev DG, Artsimovitch I. 2007. Allosteric control of the RNA polymerase by the elongation factor RfaH. Nucleic Acids Res 35:5694–5705. [PubMed][CrossRef]
82. Tomar SK, Knauer SH, Nandymazumdar M, Rosch P, Artsimovitch I. 2013. Interdomain contacts control folding of transcription factor RfaH. Nucleic Acids Res 41:10077–10085. [PubMed][CrossRef]
83. Nudler E, Gottesman ME. 2002. Transcription termination and anti-termination in E. coli. Genes Cells 7:755–768. [PubMed][CrossRef]
84. Gusarov I, Nudler E. 2001. Control of intrinsic transcription termination by N and NusA: the basic mechanisms. Cell 107:437–449. [PubMed][CrossRef]
85. Komissarova N, Becker J, Solter S, Kireeva M, Kashlev M. 2002. Shortening of RNA:DNA hybrid in the elongation complex of RNA polymerase is a prerequisite for transcription termination. Mol Cell 10:1151–1162. [PubMed][CrossRef]
86. Bermudez-Cruz RM, Chamberlin MJ, Montanez C. 1999. Nus A is involved in transcriptional termination on lambda tI. Biochimie 81:757–764. [PubMed][CrossRef]
87. Farnham PJ, Greenblatt J, Platt T. 1982. Effects of NusA protein on transcription termination in the tryptophan operon of Escherichia coli. Cell 29:945–951. [PubMed][CrossRef]
88. Schmidt MC, Chamberlin MJ. 1987. nusA protein of Escherichia coli is an efficient transcription termination factor for certain terminator sites. J Mol Biol 195:809–818. [PubMed][CrossRef]
89. Toulokhonov I, Artsimovitch I, Landick R. 2001. Allosteric control of RNA polymerase by a site that contacts nascent RNA hairpins. Science 292:730–733. [PubMed][CrossRef]
90. Rees WA, Weitzel SE, Das A, von Hippel PH. 1997. Regulation of the elongation-termination decision at intrinsic terminators by antitermination protein N of phage lambda. J Mol Biol 273:797–813. [PubMed][CrossRef]
91. Sha Y, Lindahl L, Zengel JM. 1995. Role of NusA in L4-mediated attenuation control of the S10 r-protein operon of Escherichia coli. J Mol Biol 245:474–485. [PubMed][CrossRef]
92. Sha Y, Lindahl L, Zengel JM. 1995. RNA determinants required for L4-mediated attenuation control of the S10 r-protein operon of Escherichia coli. J Mol Biol 245:486–498. [PubMed][CrossRef]
93. Zengel JM, Lindahl L. 1990. Ribosomal protein L4 stimulates in vitro termination of transcription at a NusA-dependent terminator in the S10 operon leader. Proc Natl Acad Sci USA 87:2675–2679. [PubMed][CrossRef]
94. Zengel JM, Lindahl L. 1996. A hairpin structure upstream of the terminator hairpin required for ribosomal protein L4-mediated attenuation control of the S10 operon of Escherichia coli. J Bacteriol 178:2383–2387. [PubMed]
95. Banerjee S, Chalissery J, Bandey I, Sen R. 2006. Rho-dependent transcription termination: more questions than answers. J Microbiol 44:11–22. [PubMed]
96. Bear DG, Hicks PS, Escudero KW, Andrews CL, McSwiggen JA, von Hippel PH. 1988. Interactions of Escherichia coli transcription termination factor rho with RNA. II. Electron microscopy and nuclease protection experiments. J Mol Biol 199:623–635. [PubMed][CrossRef]
97. Modrak D, Richardson JP. 1994. The RNA-binding domain of transcription termination factor rho: isolation, characterization, and determination of sequence limits. Biochemistry 33:8292–8299. [PubMed][CrossRef]
98. Kalyani BS, Muteeb G, Qayyum MZ, Sen R. 2011. Interaction with the nascent RNA is a prerequisite for the recruitment of Rho to the transcription elongation complex in vitro. J Mol Biol 413:548–560. [PubMed][CrossRef]
99. Brennan CA, Dombroski AJ, Platt T. 1987. Transcription termination factor rho is an RNA-DNA helicase. Cell 48:945–952. [PubMed][CrossRef]
100. Li J, Mason SW, Greenblatt J. 1993. Elongation factor NusG interacts with termination factor rho to regulate termination and antitermination of transcription. Genes Dev 7:161–172. [PubMed][CrossRef]
101. Sullivan SL, Gottesman ME. 1992. Requirement for E. coli NusG protein in factor-dependent transcription termination. Cell 68:994. [PubMed][CrossRef]
102. Burns CM, Nowatzke WL, Richardson JP. 1999. Activation of Rho-dependent transcription termination by NusG. Dependence on terminator location and acceleration of RNA release. J Biol Chem 274:5245–5251. [PubMed][CrossRef]
103. Nehrke KW, Zalatan F, Platt T. 1993. NusG alters rho-dependent termination of transcription in vitro independent of kinetic coupling. Gene Expr 3:119–133. [PubMed]
104. Chalissery J, Banerjee S, Bandey I, Sen R. 2007. Transcription termination defective mutants of Rho: role of different functions of Rho in releasing RNA from the elongation complex. J Mol Biol 371:855–872. [PubMed][CrossRef]
105. Schmidt MC, Chamberlin MJ. 1984. Binding of rho factor to Escherichia coli RNA polymerase mediated by nusA protein. J Biol Chem 259:15000–15002. [PubMed]
106. Kainz M, Gourse RL. 1998. The C-terminal domain of the alpha subunit of Escherichia coli RNA polymerase is required for efficient rho-dependent transcription termination. J Mol Biol 284:1379–1390. [PubMed][CrossRef]
107. Chattopadhyay S, Garcia-Mena J, DeVito J, Wolska K, Das A. 1995. Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage lambda. Proc Natl Acad Sci USA 92:4061–4065. [PubMed][CrossRef]
108. Lazinski D, Grzadzielska E, Das A. 1989. Sequence-specific recognition of RNA hairpins by bacteriophage antiterminators requires a conserved arginine-rich motif. Cell 59:207–208. [CrossRef]
109. Das A. 1993. Control of transcription termination by RNA-binding proteins. Ann Rev Biochem 62:893–930. [PubMed][CrossRef]
110. Greenblatt J, Nodwell JR, Mason SW. 1993. Transcriptional antitermination. Nature 364:401–406. [PubMed][CrossRef]
111. Mogridge J, Mah TF, Greenblatt J. 1998. Involvement of boxA nucleotides in the formation of a stable ribonucleoprotein complex containing the bacteriophage lambda N protein. J Biol Chem 273:4143–4148. [PubMed][CrossRef]
112. Friedman DI, Court DL. 1995. Transcription antitermination: the lambda paradigm updated. Mol Microbiol 18:191–200. [PubMed][CrossRef]
113. Weisberg RA, Gottesman ME. 1999. Processive antitermination. J Bacteriol 181:359–367. [PubMed]
114. Mogridge J, Legault P, Li J, Van Oene MD, Kay LE, Greenblatt J. 1998. Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein. Mol Cell 1:265–275. [PubMed][CrossRef]
115. DeVito J, Das A. 1994. Control of transcription processivity in phage lambda: Nus factors strengthen the termination-resistant state of RNA polymerase induced by N antiterminator. Proc Natl Acad Sci USA 91:8660–8664. [PubMed][CrossRef]
116. Mason SW, Greenblatt J. 1991. Assembly of transcription elongation complexes containing the N protein of phage lambda and the Escherichia coli elongation factors NusA, NusB, NusG, and S10. Genes Dev 5:1504–1512. [CrossRef]
117. Van Gilst MR, von Hippel PH. 1997. Assembly of the N-dependent antitermination complex of phage lambda: NusA and RNA bind independently to different unfolded domains of the N protein. J Mol Biol 274:160–173. [PubMed][CrossRef]
118. Zhou Y, Mah TF, Yu YT, Mogridge J, Olson ER, Greenblatt J, Friedman DI. 2001. Interactions of an Arg-rich region of transcription elongation protein NusA with NUT RNA: implications for the order of assembly of the lambda N antitermination complex in vivo. J Mol Biol 310:33–49. [PubMed][CrossRef]
119. Prasch S, Jurk M, Washburn RS, Gottesman ME, Wohrl BM, Rosch P. 2009. RNA-binding specificity of E. coli NusA. Nucleic Acids Res 37:4736–4742. [PubMed][CrossRef]
120. Mishra S, Mohan S, Godavarthi S, Sen R. 2013. The interaction surface of a bacterial transcription elongation factor required for complex formation with an antiterminator during transcription antitermination. J Biol Chem 288:28089–28103. [PubMed][CrossRef]
121. Muteeb G, Dey D, Mishra S, Sen R. 2012. A multipronged strategy of an anti-terminator protein to overcome Rho-dependent transcription termination. Nucleic Acids Res 40:11213–11228. [PubMed][CrossRef]
122. Shankar S, Hatoum A, Roberts JW. 2007. A transcription antiterminator constructs a NusA-dependent shield to the emerging transcript. Mol Cell 27:914–927. [PubMed][CrossRef]
123. Robert J, Sloan SB, Weisberg RA, Gottesman ME, Robledo R, Harbrecht D. 1987. The remarkable specificity of a new transcription termination factor suggests that the mechanisms of termination and antitermination are similar. Cell 51:483–492. [PubMed][CrossRef]
124. Hung SC, Gottesman ME. 1995. Phage HK022 Nun protein arrests transcription on phage lambda DNA in vitro and competes with the phage lambda N antitermination protein. J Mol Biol 247:428–442. [PubMed][CrossRef]
125. Kim HC, Washburn RS, Gottesman ME. 2006. Role of E.coli NusA in phage HK022 Nun-mediated transcription termination. J Mol Biol 359:10–21. [PubMed][CrossRef]
126. Watnick RS, Gottesman ME. 1999. Binding of transcription termination protein nun to nascent RNA and template DNA. Science 286:2337–2339. [PubMed][CrossRef]
127. Washburn RS, Wang Y, Gottesman ME. 2003. Role of E.coli transcription-repair coupling factor Mfd in Nun-mediated transcription termination. J Mol Biol 329:655–662. [PubMed][CrossRef]
128. Paul BJ, Ross W, Gaal T, Gourse RL. 2004. rRNA transcription in Escherichia coli. Ann Rev Genet 38:749–770. [PubMed][CrossRef]
129. Albrechtsen B, Squires CL, Li S, Squires C. 1990. Antitermination of characterized transcriptional terminators by the Escherichia coli rrnG leader region. J Mol Biol 213:123–134. [PubMed][CrossRef]
130. Zellars M, Squires CL. 1999. Antiterminator-dependent modulation of transcription elongation rates by NusB and NusG. Mol Microbiol 32:1296–1304. [PubMed][CrossRef]
131. Berg KL, Squires C, Squires CL. 1989. Ribosomal RNA operon anti-termination. Function of leader and spacer region box B-box A sequences and their conservation in diverse micro-organisms. J Mol Biol 209:345–358. [PubMed][CrossRef]
132. Li SC, Squires CL, Squires C. 1984. Antitermination of E. coli rRNA transcription is caused by a control region segment containing lambda nut-like sequences. Cell 38:851–860. [PubMed][CrossRef]
133. Burmann BM, Luo X, Rosch P, Wahl MC, Gottesman ME. 2010. Fine tuning of the E. coli NusB:NusE complex affinity to BoxA RNA is required for processive antitermination. Nucleic Acids Res 38:314–326. [PubMed][CrossRef]
134. Hu M, Nandi S, Davies C, Nicholas RA. 2005. High-level chromosomally mediated tetracycline resistance in Neisseria gonorrhoeae results from a point mutation in the rpsJ gene encoding ribosomal protein S10 in combination with the mtrR and penB resistance determinants. Antimicrob Agents Chemother 49:4327–4334. [PubMed][CrossRef]
135. Wilson HR, Kameyama L, Zhou JG, Guarneros G, Court DL. 1997. Translational repression by a transcriptional elongation factor. Genes Dev 11:2204–2213. [PubMed][CrossRef]
136. Wilson HR, Zhou JG, Yu D, Court DL. 2004. Translation repression by an RNA polymerase elongation complex. Mol Microbiol 53:821–828. [PubMed][CrossRef]
137. Friedberg EC, Walker GC, Siede W, Wood RD, Schultz RA, Ellenberger T. 2005. DNA Repair and Mutagenesis. ASM Press, Washington, DC.
138. Tornaletti S, Hanawalt PC. 1999. Effect of DNA lesions on transcription elongation. Biochimie 81:139–146. [PubMed][CrossRef]
139. Selby CP, Sancar A. 1990. Transcription preferentially inhibits nucleotide excision repair of the template DNA strand in vitro. J Biol Chem 265:21330–21336. [PubMed]
140. Savery NJ. 2007. The molecular mechanism of transcription-coupled DNA repair. Trends Microbiol 15:326–333. [PubMed][CrossRef]
141. Cohen SE, Walker GC. 2010. The transcription elongation factor NusA is required for stress-induced mutagenesis in Escherichia coli. Curr Biol 20:80–85. [PubMed][CrossRef]
142. Epshtein V, Kamarthapu V, McGary K, Svetlov V, Ueberheide B, Proshkin S, Mironov A, Nudler E. 2014. UvrD facilitates DNA repair by pulling RNA polymerase backwards. Nature 505:372–377. [PubMed][CrossRef]
143. Bubunenko M, Court DL, Al Refaii A, Saxena S, Korepanov A, Friedman DI, Gottesman ME, Alix JH. 2013. Nus transcription elongation factors and RNase III modulate small ribosome subunit biogenesis in Escherichia coli. Mol Microbiol 87:382–393. [PubMed][CrossRef]
144. Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H. 2006. Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16:686–691. [PubMed][CrossRef]
145. Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A. 2005. Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433:531–537. [PubMed][CrossRef]
146. Yellaboina S, Goyal K, Mande SC. 2007. Inferring genome-wide functional linkages in E. coli by combining improved genome context methods: comparison with high-throughput experimental data. Genome Res 17:527535. [PubMed][CrossRef]
147. Neely MN, Friedman DI. 2000. N-mediated transcription antitermination in lambdoid phage H-19B is characterized by alternative NUT RNA structures and a reduced requirement for host factors. Mol Microbiol 38:1074–1085. [PubMed][CrossRef]
148. journal-id:
Loading

Article metrics loading...

/content/journal/ecosalplus/10.1128/ecosalplus.ESP-0008-2013
2014-11-21
2020-01-21

Abstract:

The highly conserved Nus factors of bacteria were discovered as essential host proteins for the growth of temperate phage λ in . Later, their essentiality and functions in transcription, translation, and, more recently, in DNA repair have been elucidated. Close involvement of these factors in various gene networks and circuits is also emerging from recent genomic studies. We have described a detailed overview of their biochemistry, structures, and various cellular functions, as well as their interactions with other macromolecules. Towards the end, we have envisaged different uncharted areas of studies with these factors, including their participation in pathogenicity.

Highlighted Text: Show | Hide
Loading full text...

Full text loading...

Comment has been disabled for this content
Submit comment
Close
Comment moderation successfully completed

Figures

Nus Factors of
[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-1,webId=/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-1,properties={foaf_givenname=Ranjan, foaf_name=Ranjan Sen, foaf_surname=Sen, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-aff1]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-2,webId=/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-2,properties={foaf_givenname=Jisha, foaf_name=Jisha Chalissery, foaf_surname=Chalissery, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-aff2]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-3,webId=/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-3,properties={foaf_givenname=M. Zuhaib, foaf_name=M. Zuhaib Qayyum, foaf_surname=Qayyum, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-aff3]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-4,webId=/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-4,properties={foaf_givenname=V., foaf_name=V. Vishalini, foaf_surname=Vishalini, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-aff4]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-5,webId=/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-5,properties={foaf_givenname=Ghazala, foaf_name=Ghazala Muteeb, foaf_surname=Muteeb, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-aff5]]}]]
Citation: Sen R, Chalissery J, Qayyum M, Vishalini V, Muteeb G. 2014. Nus Factors of , EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0008-2013
/content/ecosalplus/10.1128/ecosalplus.ESP-0008-2013.fig1
Figure 1

Positions of the respective genes are indicated in yellow. Directions of the arrows indicate the direction of transcription. Numbers at both sides indicate the nucleotide sequences. doi:10.1128/ecosalplus.ESP-0008-2013.f1

ecosalplus/6/1/ESP-0008-2013_fig_001_thmb.gif
ecosalplus/6/1/ESP-0008-2013_fig_001.gif
Image of Figure 1
Figure 1

Positions of the respective genes are indicated in yellow. Directions of the arrows indicate the direction of transcription. Numbers at both sides indicate the nucleotide sequences. doi:10.1128/ecosalplus.ESP-0008-2013.f1

Citation: Sen R, Chalissery J, Qayyum M, Vishalini V, Muteeb G. 2014. Nus Factors of , EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0008-2013
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/ecosalplus/10.1128/ecosalplus.ESP-0008-2013.fig2
Figure 2

(A) A cartoon showing different functional domains of NusA. Domains NTD, SH, KH1/2 are highly conserved domains among different NusA molecules. Domains AR1/2 are found in few species, including . (B) Crystal structure of conserved domains of NusA from (Protein Data Bank [PDB] no. 1L2F [ 40 ]) depicts that each functional domain has distinct tertiary folds and corresponds to separate structural domains as indicated. Two separate NMR structures of AR1 and AR2 domains (PDB nos. 1WCL and 1WCN, respectively [ 36 ]) of are also shown. (C) Crystal structure of NusA (pink) with the stem-loop RNA (black) from boxC of rRNA operon (PDB no. 2ASB [ 32 ]). The structure revealed that both the RNA-binding domains KH1 and KH2 take part in the interaction with the RNA and the interaction destabilizes the stem-loop structure of boxC. (D) Solution structure of the central part of N protein (shown as a dark-green thread) from bacteriophage λ is complexed with the dimeric interface of AR1 domain of NusA (PDB no. 1U9L [ 33 ]). The dimeric interface was found to be formed from two AR1 domains coming from two NusA molecules; 352 to 419 residues of one NusA molecule (in maroon) dimerizes with the 352 to 421 residues of the second NusA molecule (light green). This indicates that, in the antitermination complex with λN, NusA may form a dimer. Amino acid numbers of the relevant region of λN protein are indicated. doi:10.1128/ecosalplus.ESP-0008-2013.f2

ecosalplus/6/1/ESP-0008-2013_fig_002_thmb.gif
ecosalplus/6/1/ESP-0008-2013_fig_002.gif
Image of Figure 2
Figure 2

(A) A cartoon showing different functional domains of NusA. Domains NTD, SH, KH1/2 are highly conserved domains among different NusA molecules. Domains AR1/2 are found in few species, including . (B) Crystal structure of conserved domains of NusA from (Protein Data Bank [PDB] no. 1L2F [ 40 ]) depicts that each functional domain has distinct tertiary folds and corresponds to separate structural domains as indicated. Two separate NMR structures of AR1 and AR2 domains (PDB nos. 1WCL and 1WCN, respectively [ 36 ]) of are also shown. (C) Crystal structure of NusA (pink) with the stem-loop RNA (black) from boxC of rRNA operon (PDB no. 2ASB [ 32 ]). The structure revealed that both the RNA-binding domains KH1 and KH2 take part in the interaction with the RNA and the interaction destabilizes the stem-loop structure of boxC. (D) Solution structure of the central part of N protein (shown as a dark-green thread) from bacteriophage λ is complexed with the dimeric interface of AR1 domain of NusA (PDB no. 1U9L [ 33 ]). The dimeric interface was found to be formed from two AR1 domains coming from two NusA molecules; 352 to 419 residues of one NusA molecule (in maroon) dimerizes with the 352 to 421 residues of the second NusA molecule (light green). This indicates that, in the antitermination complex with λN, NusA may form a dimer. Amino acid numbers of the relevant region of λN protein are indicated. doi:10.1128/ecosalplus.ESP-0008-2013.f2

Citation: Sen R, Chalissery J, Qayyum M, Vishalini V, Muteeb G. 2014. Nus Factors of , EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0008-2013
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/ecosalplus/10.1128/ecosalplus.ESP-0008-2013.fig3
Figure 3

(A) Solution structure of NusB (PDB no. 1EY1 [ 42 ]) consisting of N- and C-terminal globular domains. This solution structure shows more resemblance with the crystal structures of homologous NusBs from ( 44 ) and ( 45 ). (B) Structure of NusE (S10) when it is a part of 30S ribosome particle (chain J of the co-ordinate available from PDB no. 1J5E [ 50 ]). The RNP fold of NusE may also be important for interacting with RNA polymerase in the transcription elongation complex. doi:10.1128/ecosalplus.ESP-0008-2013.f3

ecosalplus/6/1/ESP-0008-2013_fig_003_thmb.gif
ecosalplus/6/1/ESP-0008-2013_fig_003.gif
Image of Figure 3
Figure 3

(A) Solution structure of NusB (PDB no. 1EY1 [ 42 ]) consisting of N- and C-terminal globular domains. This solution structure shows more resemblance with the crystal structures of homologous NusBs from ( 44 ) and ( 45 ). (B) Structure of NusE (S10) when it is a part of 30S ribosome particle (chain J of the co-ordinate available from PDB no. 1J5E [ 50 ]). The RNP fold of NusE may also be important for interacting with RNA polymerase in the transcription elongation complex. doi:10.1128/ecosalplus.ESP-0008-2013.f3

Citation: Sen R, Chalissery J, Qayyum M, Vishalini V, Muteeb G. 2014. Nus Factors of , EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0008-2013
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/ecosalplus/10.1128/ecosalplus.ESP-0008-2013.fig4
Figure 4

(A) Homology model of NusG ( 57 ), which is characterized by two globular domains NTD (PDB no. 2K06) and CTD (PDB no. 2JVV), connected by a flexible linker. This linker most likely ensures degrees of freedom between the two domains and their respective orientations in the space. (B) Crystal structure of RfaH (PDB no. 2OUG [ 67 ]). The sequence of NTD of RfaH is similar to that of NusG and folds in a similar way, whereas the CTD is very different: it folds into a α-helical coiled-coil structure, in contrast to the β-barrel structure of NusG, and comes over the NTD in the tertiary structure. Unlike NusG, in this conformation RfaH-CTD blocks the access of NTD. (C) Conversion of coiled-coil structure of RfaH-CTD into β-barrel structure; this transformation occurs upon interaction with EC. (D) Model of the RfaH NTD, unmasked from the CTD of RfaH, bound to the EC. Different structural elements are indicated. doi:10.1128/ecosalplus.ESP-0008-2013.f4

ecosalplus/6/1/ESP-0008-2013_fig_004_thmb.gif
ecosalplus/6/1/ESP-0008-2013_fig_004.gif
Image of Figure 4
Figure 4

(A) Homology model of NusG ( 57 ), which is characterized by two globular domains NTD (PDB no. 2K06) and CTD (PDB no. 2JVV), connected by a flexible linker. This linker most likely ensures degrees of freedom between the two domains and their respective orientations in the space. (B) Crystal structure of RfaH (PDB no. 2OUG [ 67 ]). The sequence of NTD of RfaH is similar to that of NusG and folds in a similar way, whereas the CTD is very different: it folds into a α-helical coiled-coil structure, in contrast to the β-barrel structure of NusG, and comes over the NTD in the tertiary structure. Unlike NusG, in this conformation RfaH-CTD blocks the access of NTD. (C) Conversion of coiled-coil structure of RfaH-CTD into β-barrel structure; this transformation occurs upon interaction with EC. (D) Model of the RfaH NTD, unmasked from the CTD of RfaH, bound to the EC. Different structural elements are indicated. doi:10.1128/ecosalplus.ESP-0008-2013.f4

Citation: Sen R, Chalissery J, Qayyum M, Vishalini V, Muteeb G. 2014. Nus Factors of , EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0008-2013
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/ecosalplus/10.1128/ecosalplus.ESP-0008-2013.fig5
Figure 5

(A) The gene organization of early transcription region of lambdoid phages. Transcripts originated from PL and PR promoters get prematurely terminated at T and T terminators in the absence of N protein. N protein together with a battery of Nus factors recognize the boxA and boxB elements of the RNA coded by sites. The nature and sequences of these conserved elements are described for different lambdoid phages (adapted from Figure 2 of reference 147 ). (B) A cartoon showing the assembly of N-antitermination complex on the site. Interactions of NusB/NusE heterodimer with boxA, N-terminal of N with BoxB, and N with AR1 region of NusA have been experimentally verified. Other interaction sites in the complex are not proven experimentally. doi:10.1128/ecosalplus.ESP-0008-2013.f5

ecosalplus/6/1/ESP-0008-2013_fig_005_thmb.gif
ecosalplus/6/1/ESP-0008-2013_fig_005.gif
Image of Figure 5
Figure 5

(A) The gene organization of early transcription region of lambdoid phages. Transcripts originated from PL and PR promoters get prematurely terminated at T and T terminators in the absence of N protein. N protein together with a battery of Nus factors recognize the boxA and boxB elements of the RNA coded by sites. The nature and sequences of these conserved elements are described for different lambdoid phages (adapted from Figure 2 of reference 147 ). (B) A cartoon showing the assembly of N-antitermination complex on the site. Interactions of NusB/NusE heterodimer with boxA, N-terminal of N with BoxB, and N with AR1 region of NusA have been experimentally verified. Other interaction sites in the complex are not proven experimentally. doi:10.1128/ecosalplus.ESP-0008-2013.f5

Citation: Sen R, Chalissery J, Qayyum M, Vishalini V, Muteeb G. 2014. Nus Factors of , EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0008-2013
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/ecosalplus/10.1128/ecosalplus.ESP-0008-2013.fig6
Figure 6

(A) Typical organization of an rRNA operon coding for 16S, 23S, and 5S RNAs. The antitermination signal (AT) present in the leader and spacer regions are described. The major elements (boxB-A-C) that are recognized by the different components of the antitermination complex are shown. (B) Cartoon showing the assembly of different Nus factors and ribosomal proteins on the boxA element of rRNA is described. Also shown is the transcription terminator Rho in the context of this antitermination complex. This complex helps the RNA polymerase to overcome the Rho-dependent RNA release either by increasing the elongation speed or by blocking the access of Rho, or by both the mechanisms doi:10.1128/ecosalplus.ESP-0008-2013.f6

ecosalplus/6/1/ESP-0008-2013_fig_006_thmb.gif
ecosalplus/6/1/ESP-0008-2013_fig_006.gif
Image of Figure 6
Figure 6

(A) Typical organization of an rRNA operon coding for 16S, 23S, and 5S RNAs. The antitermination signal (AT) present in the leader and spacer regions are described. The major elements (boxB-A-C) that are recognized by the different components of the antitermination complex are shown. (B) Cartoon showing the assembly of different Nus factors and ribosomal proteins on the boxA element of rRNA is described. Also shown is the transcription terminator Rho in the context of this antitermination complex. This complex helps the RNA polymerase to overcome the Rho-dependent RNA release either by increasing the elongation speed or by blocking the access of Rho, or by both the mechanisms doi:10.1128/ecosalplus.ESP-0008-2013.f6

Citation: Sen R, Chalissery J, Qayyum M, Vishalini V, Muteeb G. 2014. Nus Factors of , EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0008-2013
Permissions and Reprints Request Permissions
Download as Powerpoint

Tables

Nus Factors of
[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-1,webId=/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-1,properties={foaf_givenname=Ranjan, foaf_name=Ranjan Sen, foaf_surname=Sen, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-aff1]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-2,webId=/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-2,properties={foaf_givenname=Jisha, foaf_name=Jisha Chalissery, foaf_surname=Chalissery, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-aff2]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-3,webId=/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-3,properties={foaf_givenname=M. Zuhaib, foaf_name=M. Zuhaib Qayyum, foaf_surname=Qayyum, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-aff3]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-4,webId=/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-4,properties={foaf_givenname=V., foaf_name=V. Vishalini, foaf_surname=Vishalini, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-aff4]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-5,webId=/content/author/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-5,properties={foaf_givenname=Ghazala, foaf_name=Ghazala Muteeb, foaf_surname=Muteeb, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/ecosalplus/10.1128/ecosalplus.ESP-0008-2013-aff5]]}]]
Citation: Sen R, Chalissery J, Qayyum M, Vishalini V, Muteeb G. 2014. Nus Factors of , EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0008-2013
/content/ecosalplus/10.1128/ecosalplus.ESP-0008-2013.T1
Table 1

Summary of different properties of Nus factors

Generic image for table
Table 1

Summary of different properties of Nus factors

Citation: Sen R, Chalissery J, Qayyum M, Vishalini V, Muteeb G. 2014. Nus Factors of , EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0008-2013

Supplemental Material

No supplementary material available for this content.

Back to top
This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error