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.

The IS/IS Family and “Peel and Paste” Single-strand Transposition Mechanism

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.
  • XML
    123.26 Kb
  • HTML
    142.86 Kb
  • PDF
    1.31 MB
  • Authors: S. He1, A. Corneloup2, C. Guynet3, L. Lavatine4, A. Caumont-Sarcos5, P. Siguier6, B. Marty7, F. Dyda8, M. Chandler9, B. Ton Hoang10
  • Editors: Mick Chandler11, Nancy Craig12
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Laboratoire de Microbiologie et Génétique Moléculaires, CNRS, Toulouse, France; 2: Laboratoire de Microbiologie et Génétique Moléculaires, CNRS, Toulouse, France; 3: Laboratoire de Microbiologie et Génétique Moléculaires, CNRS, Toulouse, France; 4: Laboratoire de Microbiologie et Génétique Moléculaires, CNRS, Toulouse, France; 5: Laboratoire de Microbiologie et Génétique Moléculaires, CNRS, Toulouse, France; 6: Laboratoire de Microbiologie et Génétique Moléculaires, CNRS, Toulouse, France; 7: Laboratoire de Microbiologie et Génétique Moléculaires, CNRS, Toulouse, France; 8: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, MD; 9: Laboratoire de Microbiologie et Génétique Moléculaires, CNRS, Toulouse, France; 10: Laboratoire de Microbiologie et Génétique Moléculaires, CNRS, Toulouse, France; 11: Université Paul Sabatier, Toulouse, France; 12: Johns Hopkins University, Baltimore, MD
    • Source: microbiolspec July 2015 vol. 3 no. 4 doi:10.1128/microbiolspec.MDNA3-0039-2014
  • Received 28 July 2014 Accepted 25 February 2015 Published 02 July 2015
  • Bao Ton Hoang, [email protected]
image of The IS<span class="jp-italic">200</span>/IS<span class="jp-italic">605</span> Family and “Peel and Paste” Single-strand Transposition Mechanism
    Preview this microbiology spectrum article:
    Preview Magnify
    Zoom in
    Zoomout

    The IS/IS Family and “Peel and Paste” Single-strand Transposition Mechanism, Page 1 of 2

    | /docserver/preview/fulltext/microbiolspec/3/4/MDNA3-0039-2014-1.gif /docserver/preview/fulltext/microbiolspec/3/4/MDNA3-0039-2014-2.gif

  • Abstract:

    This chapter presents an analysis of the organization and distribution of the IS/IS family of insertion sequences (IS). Members of this family are widespread in both bacteria and archaea. They are unusual because they use obligatory single-strand DNA intermediates, which distinguishes them from classical IS. We summarize studies of the experimental model systems IS (from ) and IS (from ) and present biochemical, genetic, and structural data that describe their transposition pathway and the way in which their transposase (an HuH rather than a DDE enzyme) catalyzes this process. The transposition of IS/IS family members can be described as a “Peel-and-Paste” mechanism. We also address the probable domestication of IS/IS family transposases as enzymes involved in multiplication of repeated extragenic palindromes and as potential homing endonucleases in intron–IS chimeras.

  • Citation: He S, Corneloup A, Guynet C, Lavatine L, Caumont-Sarcos A, Siguier P, Marty B, Dyda F, Chandler M, Ton Hoang B. 2015. The IS/IS Family and “Peel and Paste” Single-strand Transposition Mechanism. Microbiol Spectrum 3(4):MDNA3-0039-2014. doi:10.1128/microbiolspec.MDNA3-0039-2014.

References

1. Chandler M, de la Cruz F, Dyda F, Hickman AB, Moncalian G, Ton-Hoang B. 2013. Breaking and joining single-stranded DNA: the HUH endonuclease superfamily. Nat Rev Microbiol 11:525–538. [PubMed][CrossRef]
2. Lam S, Roth JR. 1983. IS200: a Salmonella-specific insertion sequence. Cell 34:951–960. [PubMed][CrossRef]
3. Kersulyte D, Velapatino B, Dailide G, Mukhopadhyay AK, Ito Y, Cahuayme L, Parkinson AJ, Gilman RH, Berg DE. 2002. Transposable element ISHp608 of Helicobacter pylori: nonrandom geographic distribution, functional organization, and insertion specificity. J Bacteriol 184:992–1002. [PubMed][CrossRef]
4. Kersulyte D, Akopyants NS, Clifton SW, Roe BA, Berg DE. 1998. Novel sequence organization and insertion specificity of IS605 and IS606: chimaeric transposable elements of Helicobacter pylori. Gene 223:175–186. [PubMed][CrossRef]
5. Ton-Hoang B, Guynet C, Ronning DR, Cointin-Marty B, Dyda F, Chandler M. 2005. Transposition of ISHp608, member of an unusual family of bacterial insertion sequences. Embo J 24:3325–3338. [PubMed][CrossRef]
6. Ronning DR, Guynet C, Ton-Hoang B, Perez ZN, Ghirlando R, Chandler M, Dyda F. 2005. Active site sharing and subterminal hairpin recognition in a new class of DNA transposases. Mol Cell 20:143–154. [PubMed][CrossRef]
7. Guynet C, Hickman AB, Barabas O, Dyda F, Chandler M, Ton-Hoang B. 2008. In vitro reconstitution of a single-stranded transposition mechanism of IS608. Mol Cell 29:302–312. [PubMed][CrossRef]
8. Barabas O, Ronning DR, Guynet C, Hickman AB, Ton-Hoang B, Chandler M, Dyda F. 2008. Mechanism of IS200/IS605 family DNA transposases: activation and transposon-directed target site selection. Cell 132:208–220. [PubMed][CrossRef]
9. Pasternak C, Ton-Hoang B, Coste G, Bailone A, Chandler M, Sommer S. 2010. Irradiation-induced Deinococcus radiodurans genome fragmentation triggers transposition of a single resident insertion sequence. PLoS Genet 6:e1000799. [PubMed][CrossRef]
10. Hickman AB, James JA, Barabas O, Pasternak C, Ton-Hoang B, Chandler M, Sommer S, Dyda F. 2010. DNA recognition and the precleavage state during single-stranded DNA transposition in D. radiodurans. Embo J 29:3840–3852. [PubMed][CrossRef]
11. Devalckenaere A, Odaert M, Trieu-Cuot P, Simonet M. 1999. Characterization of IS1541-like elements in Yersinia enterocolitica and Yersinia pseudotuberculosis. FEMS Microbiol Lett 176:229–233. [PubMed][CrossRef]
12. Beuzon CR, Chessa D, Casadesus J. 2004. IS200: an old and still bacterial transposon. Int Microbiol 7:3–12. [PubMed]
13. Bisercic M, Ochman H. 1993. The ancestry of insertion sequences common to Escherichia coli and Salmonella typhimurium. J Bacteriol 175:7863–7868. [PubMed]
14. Lam S, Roth JR. 1986. Structural and functional studies of insertion element IS200. J Mol Biol 187:157–167. [PubMed][CrossRef]
15. Beuzon CR, Casadesus J. 1997. Conserved structure of IS200 elements in Salmonella. Nucleic Acids Res 25:1355–1361. [PubMed][CrossRef]
16. Beuzon CR, Marques S, Casadesus J. 1999. Repression of IS200 transposase synthesis by RNA secondary structures. Nucleic Acids Res 27:3690–3695. [PubMed][CrossRef]
17. Sittka A, Lucchini S, Papenfort K, Sharma CM, Rolle K, Binnewies TT, Hinton JCD, Vogel Jr. 2008. Deep sequencing analysis of small noncoding RNA and mRNA targets of the global post-transcriptional regulator, Hfq. PLoS Genetics 4:e1000163. [PubMed][CrossRef]
18. Odaert M, Devalckenaere A, Trieu-Cuot P, Simonet M. 1998. Molecular characterization of IS1541 insertions in the genome of Yersinia pestis. J Bacteriol 180:178–181. [PubMed]
19. Kersulyte D, Mukhopadhyay AK, Shirai M, Nakazawa T, Berg DE. 2000. Functional organization and insertion specificity of IS607, a chimeric element of Helicobacter pylori. J Bacteriol 182:5300–5308. [PubMed][CrossRef]
20. Boocock MR, Rice PA. 2013. A proposed mechanism for IS607-family serine transposases. Mob DNA 4:24. [PubMed][CrossRef]
21. Akopyants NS, Clifton SW, Kersulyte D, Crabtree JE, Youree BE, Reece CA, Bukanov NO, Drazek ES, Roe BA, Berg DE. 1998. Analyses of the cag pathogenicity island of Helicobacter pylori. Mol Microbiol 28:37–53. [PubMed][CrossRef]
22. Islam SM, Hua Y, Ohba H, Satoh K, Kikuchi M, Yanagisawa T, Narumi I. 2003. Characterization and distribution of IS8301 in the radioresistant bacterium Deinococcus radiodurans. Genes Genet Syst 78:319–327. [PubMed][CrossRef]
23. Zahradka K, Slade D, Bailone A, Sommer S, Averbeck D, Petranovic M, Lindner AB, Radman M. 2006. Reassembly of shattered chromosomes in Deinococcus radiodurans. Nature 443:569–573. [PubMed][CrossRef]
24. Murai N, Kamata H, Nagashima Y, Yagisawa H, Hirata H. 1995. A novel insertion sequence (IS)-like element of the thermophilic bacterium PS3 promotes expression of the alanine carrier protein-encoding gene. Gene 163:103–107. [PubMed][CrossRef]
25. Bancroft I, Wolk CP. 1989. Characterization of an insertion sequence (IS891) of novel structure from the cyanobacterium Anabaena sp. strain M-131. J Bacteriol 171:5949–5954. [PubMed]
26. Stanley TL, Ellermeier CD, Slauch JM. 2000. Tissue-specific gene expression identifies a gene in the lysogenic phage Gifsy-1 that affects Salmonella enterica serovar typhimurium survival in Peyer's patches. J Bacteriol 182:4406–4413. [PubMed][CrossRef]
27. Ton-Hoang B, Pasternak C, Siguier P, Guynet C, Hickman AB, Dyda F, Sommer S, Chandler M. 2010. Single-stranded DNA transposition is coupled to host replication. Cell 142:398–408. [PubMed][CrossRef]
28. Koonin EV, Ilyina TV. 1993. Computer-assisted dissection of rolling circle DNA replication. Biosystems 30:241–268. [PubMed][CrossRef]
29. Lee HH, Yoon JY, Kim HS, Kang JY, Kim KH, Kim do J, Ha JY, Mikami B, Yoon HJ, Suh SW. 2006. Crystal structure of a metal ion-bound IS200 transposase. J Biol Chem 281:4261–4266. [PubMed][CrossRef]
30. He S, Guynet C, Siguier P, Hickman AB, Dyda F, Chandler M, Ton-Hoang B. 2013. IS200/IS605 family single-strand transposition: mechanism of IS608 strand transfer. Nucleic Acids Res 41:3302–3313. [PubMed][CrossRef]
31. He S, Hickman AB, Dyda F, Johnson NP, Chandler M, Ton-Hoang B. 2011. Reconstitution of a functional IS608 single-strand transpososome: role of non-canonical base pairing. Nucleic Acids Res 39:8503–8512. [PubMed][CrossRef]
32. Guynet C, Achard A, Hoang BT, Barabas O, Hickman AB, Dyda F, Chandler M. 2009. Resetting the site: redirecting integration of an insertion sequence in a predictable way. Mol Cell 34:612–619. [PubMed][CrossRef]
33. Mennecier S, Servant P, Coste G, Bailone A, Sommer S. 2006. Mutagenesis via IS transposition in Deinococcus radiodurans. Mol Microbiol 59:317–325. [PubMed][CrossRef]
34. Parks AR, Li Z, Shi Q, Owens RM, Jin MM, Peters JE. 2009. Transposition into replicating DNA occurs through interaction with the processivity factor. Cell 138:685–695. [PubMed][CrossRef]
35. Hu WY, Derbyshire KM. 1998. Target choice and orientation preference of the insertion sequence IS903. J Bacteriol 180:3039–3048. [PubMed]
36. Roberts D, Hoopes BC, McClure WR, Kleckner N. 1985. IS10 transposition is regulated by DNA adenine methylation. Cell 43:117–130. [PubMed][CrossRef]
37. Yin JC, Krebs MP, Reznikoff WS. 1988. Effect of dam methylation on Tn5 transposition. J Mol Biol 199:35–45. [PubMed][CrossRef]
38. Dodson KW, Berg DE. 1989. Factors affecting transposition activity of IS50 and Tn5 ends. Gene 76:207–213. [PubMed][CrossRef]
39. Spradling AC, Bellen HJ, Hoskins RA. 2011. Drosophila P elements preferentially transpose to replication origins. Proc Natl Acad Sci U S A 108:15948–15953. [PubMed][CrossRef]
40. Zechner EL, Wu CA, Marians KJ. 1992. Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. II. Frequency of primer synthesis and efficiency of primer utilization control Okazaki fragment size. J Biol Chem 267:4045–4053. [PubMed]
41. Wu CA, Zechner EL, Reems JA, McHenry CS, Marians KJ. 1992. Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. V. Primase action regulates the cycle of Okazaki fragment synthesis. J Biol Chem 267:4074–4083. [PubMed]
42. Lau IF, Filipe SR, Soballe B, Okstad OA, Barre FX, Sherratt DJ. 2003. Spatial and temporal organization of replicating Escherichia coli chromosomes. Mol Microbiol 49:731–743. [PubMed][CrossRef]
43. Hansen MT. 1978. Multiplicity of genome equivalents in the radiation-resistant bacterium Micrococcus radiodurans. J Bacteriol 134:71–75. [PubMed]
44. Harsojo, Kitayama S, Matsuyama A. 1981. Genome multiplicity and radiation resistance in Micrococcus radiodurans. J Biochem 90:877–880. [PubMed]
45. Pasternak C, Dulermo R, Ton-Hoang B, Debuchy R, Siguier P, Coste G, Chandler M, Sommer S. 2013. ISDra2 transposition in Deinococcus radiodurans is downregulated by TnpB. Mol Microbiol 88:443–455. [PubMed][CrossRef]
46. Krishna SS, Majumdar I, Grishin NV. 2003. Structural classification of zinc fingers: survey and summary. Nucleic Acids Res 31:532–550. [PubMed][CrossRef]
47. Gilbert C, Cordaux R. 2013. Horizontal transfer and evolution of prokaryote transposable elements in eukaryotes. Genome Biol Evol 5:822–832. [PubMed][CrossRef]
48. Filée J, Siguier P, Chandler M. 2007. I am what I eat and I eat what I am: acquisition of bacterial genes by giant viruses. Trends Genet 23:10–15. [PubMed][CrossRef]
49. Bao W, Jurka J. 2013. Homologues of bacterial TnpB_IS605 are widespread in diverse eukaryotic transposable elements. Mob DNA 4:12. [PubMed][CrossRef]
50. Volff JN. 2006. Turning junk into gold: domestication of transposable elements and the creation of new genes in eukaryotes. Bioessays 28:913–922. [PubMed][CrossRef]
51. Vogt A, Goldman AD, Mochizuki K, Landweber LF. 2013. Transposon domestication versus mutualism in ciliate genome rearrangements. PLoS Genet 9:e1003659. [PubMed][CrossRef]
52. Nunvar J, Huckova T, Licha I. 2010. Identification and characterization of repetitive extragenic palindromes (REP)-associated tyrosine transposases: implications for REP evolution and dynamics in bacterial genomes. BMC Genomics 11:44. [PubMed][CrossRef]
53. Ton-Hoang B, Siguier P, Quentin Y, Onillon S, Marty B, Fichant G, Chandler M. 2012. Structuring the bacterial genome: Y1-transposases associated with REP-BIME sequences. Nucleic Acids Res 40:3596–3609. [PubMed][CrossRef]
54. Rocco F, De Gregorio E, Di Nocera PP. 2010. A giant family of short palindromic sequences in Stenotrophomonas maltophilia. FEMS Microbiol Lett 308:185–192. [PubMed][CrossRef]
55. Nunvar J, Licha I, Schneider B. 2013. Evolution of REP diversity: a comparative study. BMC Genomics 14:385. [PubMed][CrossRef]
56. Gilson E, Bachellier S, Perrin S, Perrin D, Grimont PA, Grimont F, Hofnung M. 1990. Palindromic unit highly repetitive DNA sequences exhibit species specificity within Enterobacteriaceae. Res Microbiol 141:1103–1116. [PubMed][CrossRef]
57. Boccard F, Prentki P. 1993. Specific interaction of IHF with RIBs, a class of bacterial repetitive DNA elements located at the 3′ end of transcription units. Embo J 12:5019–5027. [PubMed]
58. Espeli O, Boccard F. 1997. In vivo cleavage of Escherichia coli BIME-2 repeats by DNA gyrase: genetic characterization of the target and identification of the cut site. Mol Microbiol 26:767–777. [PubMed][CrossRef]
59. Gilson E, Perrin D, Hofnung M. 1990. DNA polymerase I and a protein complex bind specifically to E. coli palindromic unit highly repetitive DNA: implications for bacterial chromosome organization. Nucleic Acids Res 18:3941–3952. [PubMed][CrossRef]
60. Khemici V, Carpousis AJ. 2004. The RNA degradosome and poly(A) polymerase of Escherichia coli are required in vivo for the degradation of small mRNA decay intermediates containing REP-stabilizers. Mol Microbiol 51:777–790. [PubMed][CrossRef]
61. Tobes R, Pareja E. 2006. Bacterial repetitive extragenic palindromic sequences are DNA targets for Insertion Sequence elements. BMC Genomics 7:62. [PubMed][CrossRef]
62. Ton-Hoang B, Siguier P, Quentin Y, Onillon S, Marty B, Fichant G, Chandler M. 2012. Structuring the bacterial genome: Y1-transposases associated with REP-BIME sequences. Nucleic Acids Res 40:3596–3609. [PubMed][CrossRef]
63. Messing SA, Ton-Hoang B, Hickman AB, McCubbin AJ, Peaslee GF, Ghirlando R, Chandler M, Dyda F. 2012. The processing of repetitive extragenic palindromes: the structure of a repetitive extragenic palindrome bound to its associated nuclease. Nucleic Acids Res 40:9964–9979. [PubMed][CrossRef]
64. Braun V, Mehlig M, Moos M, Rupnik M, Kalt B, Mahony DE, von Eichel-Streiber C. 2000. A chimeric ribozyme in Clostridium difficile combines features of group I introns and insertion elements. Mol Microbiol 36:1447–1459. [PubMed][CrossRef]
65. Tourasse NJ, Helgason E, Okstad OA, Hegna IK, Kolsto AB. 2006. The Bacillus cereus group: novel aspects of population structure and genome dynamics. J Appl Microbiol 101:579–593. [PubMed][CrossRef]
66. Nielsen H, Johansen SD. 2009. Group I introns: moving in new directions. RNA Biol 6:375–383. [PubMed][CrossRef]
67. Tourasse NJ, Stabell FB, Kolsto AB. 2014. Survey of chimeric IStron elements in bacterial genomes: multiple molecular symbioses between group I intron ribozymes and DNA transposons. Nucleic Acids Res 42:12333–12351. [PubMed][CrossRef]
Loading

Article metrics loading...

/content/journal/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014
2015-07-02
2021-04-17

Abstract:

This chapter presents an analysis of the organization and distribution of the IS/IS family of insertion sequences (IS). Members of this family are widespread in both bacteria and archaea. They are unusual because they use obligatory single-strand DNA intermediates, which distinguishes them from classical IS. We summarize studies of the experimental model systems IS (from ) and IS (from ) and present biochemical, genetic, and structural data that describe their transposition pathway and the way in which their transposase (an HuH rather than a DDE enzyme) catalyzes this process. The transposition of IS/IS family members can be described as a “Peel-and-Paste” mechanism. We also address the probable domestication of IS/IS family transposases as enzymes involved in multiplication of repeated extragenic palindromes and as potential homing endonucleases in intron–IS chimeras.

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

Full text loading...

/deliver/fulltext/microbiolspec/3/4/MDNA3-0039-2014.html?itemId=/content/journal/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014&mimeType=html&fmt=ahah

Figures

The IS/IS Family and “Peel and Paste” Single-strand Transposition Mechanism
[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-1,webId=/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-1,properties={foaf_givenname=S., foaf_name=S. He, foaf_surname=He, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-aff1]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-2,webId=/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-2,properties={foaf_givenname=A., foaf_name=A. Corneloup, foaf_surname=Corneloup, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-aff2]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-3,webId=/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-3,properties={foaf_givenname=C., foaf_name=C. Guynet, foaf_surname=Guynet, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-aff3]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-4,webId=/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-4,properties={foaf_givenname=L., foaf_name=L. Lavatine, foaf_surname=Lavatine, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-aff4]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-5,webId=/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-5,properties={foaf_givenname=A., foaf_name=A. Caumont-Sarcos, foaf_surname=Caumont-Sarcos, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-aff5]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-6,webId=/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-6,properties={foaf_givenname=P., foaf_name=P. Siguier, foaf_surname=Siguier, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-aff6]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-7,webId=/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-7,properties={foaf_givenname=B., foaf_name=B. Marty, foaf_surname=Marty, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-aff7]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-8,webId=/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-8,properties={foaf_givenname=F., foaf_name=F. Dyda, foaf_surname=Dyda, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-aff8]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-9,webId=/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-9,properties={foaf_givenname=M., foaf_name=M. Chandler, foaf_surname=Chandler, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-aff9]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-10,webId=/content/author/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-10,properties={foaf_givenname=B., foaf_name=B. Ton Hoang, foaf_surname=Ton Hoang, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014-aff10]]}]]
Citation: He S, Corneloup A, Guynet C, Lavatine L, Caumont-Sarcos A, Siguier P, Marty B, Dyda F, Chandler M, Ton Hoang B. 2015. The is/is family and “peel and paste” single-strand transposition mechanism. microbiolspec 3(4): doi:10.1128/microbiolspec.MDNA3-0039-2014
/content/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014.fig1
FIGURE 1
Organization of IS/IS family. (A) Genetic organization. Left (LE) and right (RE) ends carrying the subterminal hairpin (HP) are presented as red and blue boxes, respectively (colour code retained throughout). Left and right cleavage sites (C and C) are presented as black and blue boxes respectively, where the black box also represents element-specific tetra-/pentanucleotide target site (T). The cleavage positions are indicated by small vertical arrows. Gray arrows: and open reading frames (s); (i) IS group with alone; (ii) to (iv) IS group with and in different configurations; (v) IS group with alone. (B) IS. Secondary structures in the LE, adapted from reference 16 : promoter (p), ribosome binding site (RBS), start and stop codons (AUG and UAA) are indicated. (i) DNA top strand with perfect palindromes at LE and RE in red and blue, interior stem–loop in black, (ii) RNA stem–loop structure in transcript originated from p. (C) Organization of TnpB protein and derivatives: putative N-terminal helix-turn-helix motif (HTH), central OrfB_IS domain with a putative DDE motif (Pfam) and C-terminal zinc finger motif (ZF) are shown. Numbers represent occurrence of corresponding variants among 85 analyzed sequences: 46 carry all the three domains (e.g., IS), 33 lack HTH motif (e.g., IS), whereas others retain separate domains.
microbiolspec/3/4/MDNA3-0039-2014-fig1_thmb.gif
microbiolspec/3/4/MDNA3-0039-2014-fig1.gif
Image of FIGURE 1

Click to view

FIGURE 1

Organization of IS/IS family. (A) Genetic organization. Left (LE) and right (RE) ends carrying the subterminal hairpin (HP) are presented as red and blue boxes, respectively (colour code retained throughout). Left and right cleavage sites (C and C) are presented as black and blue boxes respectively, where the black box also represents element-specific tetra-/pentanucleotide target site (T). The cleavage positions are indicated by small vertical arrows. Gray arrows: and open reading frames (s); (i) IS group with alone; (ii) to (iv) IS group with and in different configurations; (v) IS group with alone. (B) IS. Secondary structures in the LE, adapted from reference 16 : promoter (p), ribosome binding site (RBS), start and stop codons (AUG and UAA) are indicated. (i) DNA top strand with perfect palindromes at LE and RE in red and blue, interior stem–loop in black, (ii) RNA stem–loop structure in transcript originated from p. (C) Organization of TnpB protein and derivatives: putative N-terminal helix-turn-helix motif (HTH), central OrfB_IS domain with a putative DDE motif (Pfam) and C-terminal zinc finger motif (ZF) are shown. Numbers represent occurrence of corresponding variants among 85 analyzed sequences: 46 carry all the three domains (e.g., IS), 33 lack HTH motif (e.g., IS), whereas others retain separate domains.

Source: microbiolspec July 2015 vol. 3 no. 4 doi:10.1128/microbiolspec.MDNA3-0039-2014
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014.fig2
FIGURE 2
IS and transposition cycle. IS organization. The left (LE) and right (RE) ends with subterminal hairpin (HP) are in red and blue, left and right cleavage sites (C/T and C) are represented by black and blue boxes, respectively. Excision. (A) TnpA activity: top strand (active strand) structures are recognized and cleaved by TnpA (vertical arrows). (B) Upon cleavage, a 5′ phosphotyrosine bond (green cylinder) is formed with LE and with the RE 3′ flank and 3′-OH (yellow circle) is formed at left flank and RE. (C) Excision of the IS single-strand circle intermediate with abutted LE and RE (RE–LE junction or transposon joint) (C) accompanied by formation of donor joint retaining the target sequence. (D) The transposase catalyzes the cleavage of transposon joint and single-strand target (E) then integration (F).
microbiolspec/3/4/MDNA3-0039-2014-fig2_thmb.gif
microbiolspec/3/4/MDNA3-0039-2014-fig2.gif
Image of FIGURE 2

Click to view

FIGURE 2

IS and transposition cycle. IS organization. The left (LE) and right (RE) ends with subterminal hairpin (HP) are in red and blue, left and right cleavage sites (C/T and C) are represented by black and blue boxes, respectively. Excision. (A) TnpA activity: top strand (active strand) structures are recognized and cleaved by TnpA (vertical arrows). (B) Upon cleavage, a 5′ phosphotyrosine bond (green cylinder) is formed with LE and with the RE 3′ flank and 3′-OH (yellow circle) is formed at left flank and RE. (C) Excision of the IS single-strand circle intermediate with abutted LE and RE (RE–LE junction or transposon joint) (C) accompanied by formation of donor joint retaining the target sequence. (D) The transposase catalyzes the cleavage of transposon joint and single-strand target (E) then integration (F).

Source: microbiolspec July 2015 vol. 3 no. 4 doi:10.1128/microbiolspec.MDNA3-0039-2014
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014.fig3
FIGURE 3
TnpA structures (adapted from references 6 and 8 ). (A) Crystallographic structure of TnpA alone. The two monomers of the TnpA dimer are colored green and orange, respectively. Positions of helix αD and catalytic residues are shown. (B) Costructure TnpA–RE HP22. HP22 is shown in blue. The extrahelical T17 and the T located in the hairpin loop are indicated in red ( 6 ). Note that in the TnpA–HP22 costructure, binding sites for the hairpins are located on the same face of the TnpA dimer whereas the two catalytic sites are formed on the opposite surface (A, C–F). (C) Configuration of the active site in the TnpA–RE HP22. HP22 is shown in blue. Note that in A, B and C, TnpA is in the inactive conformation. The arrow shows the presumed rotation of the αD helix to activate the protein. (D) Configuration of the active site in the TnpA–LE HP26 costructure. LE HP26 is shown in red and the 5′ 4-nucleotide extension (G) in yellow). The base A+18 has displaced Y127 to activate the protein. (E) TnpA–RE35 complex. Interaction of G-C (in light and dark blue, respectively) positions the cleavage site within the catalytic site of the protein. (F) Modeled TnpA–LE–RE complex. LE, RE, and flanking sequences in red, blue, and black, respectively.
microbiolspec/3/4/MDNA3-0039-2014-fig3_thmb.gif
microbiolspec/3/4/MDNA3-0039-2014-fig3.gif
Image of FIGURE 3

Click to view

FIGURE 3

TnpA structures (adapted from references 6 and 8 ). (A) Crystallographic structure of TnpA alone. The two monomers of the TnpA dimer are colored green and orange, respectively. Positions of helix αD and catalytic residues are shown. (B) Costructure TnpA–RE HP22. HP22 is shown in blue. The extrahelical T17 and the T located in the hairpin loop are indicated in red ( 6 ). Note that in the TnpA–HP22 costructure, binding sites for the hairpins are located on the same face of the TnpA dimer whereas the two catalytic sites are formed on the opposite surface (A, C–F). (C) Configuration of the active site in the TnpA–RE HP22. HP22 is shown in blue. Note that in A, B and C, TnpA is in the inactive conformation. The arrow shows the presumed rotation of the αD helix to activate the protein. (D) Configuration of the active site in the TnpA–LE HP26 costructure. LE HP26 is shown in red and the 5′ 4-nucleotide extension (G) in yellow). The base A+18 has displaced Y127 to activate the protein. (E) TnpA–RE35 complex. Interaction of G-C (in light and dark blue, respectively) positions the cleavage site within the catalytic site of the protein. (F) Modeled TnpA–LE–RE complex. LE, RE, and flanking sequences in red, blue, and black, respectively.

Source: microbiolspec July 2015 vol. 3 no. 4 doi:10.1128/microbiolspec.MDNA3-0039-2014
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014.fig4
FIGURE 4a
Recognition of cleavage sites. Schematic of the canonical and noncanonical base interactions in (A) left end (LE) and (B) right end (RE). The LE and RE are shown in red and blue. Cleavage sequences C or C are placed in black or dark blue boxes; guide sequences G and G are framed in pink and light blue, respectively. Two nucleotides at the 3′ foot of HP involved in triplet formation are highlighted by bold and in black frame. Nucleotide sequences of LE and RE and the base paring within HP and HP are shown. The inset figures describe the interactions between the cleavage sequences and guide sequences. The filled lines indicate canonical base interactions and the dotted lines indicate additional noncanonical base interactions. (C) Structure of the co-complex TnpA–RE35 adapted from reference 8 showing the active site and the base pairs between C (TCAA, dark blue) and G (GAAT, light blue). The gray sphere is bound Mn. Right: Two base triplets observed in the TnpA–RE35 complex. (D) Target recognition: single-strand transposon joint (RE–LE junction) and target Ts are presented. For simplicity only the recognition of the target cleavage site is indicated. (E) Cleavage sites recognition in the IS/IS family. Multiple sequence alignment of the cleavage sites and guide sequences using Weblogo (weblogo.berkeley.edu) was carried out on 38, 43 and 23 members of the IS (i), the IS (ii), and the IS (iii) groups, respectively. (F) Linker length distribution of LE and RE from 76 (red) and 80 (blue) different IS, respectively.
microbiolspec/3/4/MDNA3-0039-2014-fig4a_thmb.gif
microbiolspec/3/4/MDNA3-0039-2014-fig4a.gif
Image of FIGURE 4a

Click to view

FIGURE 4a

Recognition of cleavage sites. Schematic of the canonical and noncanonical base interactions in (A) left end (LE) and (B) right end (RE). The LE and RE are shown in red and blue. Cleavage sequences C or C are placed in black or dark blue boxes; guide sequences G and G are framed in pink and light blue, respectively. Two nucleotides at the 3′ foot of HP involved in triplet formation are highlighted by bold and in black frame. Nucleotide sequences of LE and RE and the base paring within HP and HP are shown. The inset figures describe the interactions between the cleavage sequences and guide sequences. The filled lines indicate canonical base interactions and the dotted lines indicate additional noncanonical base interactions. (C) Structure of the co-complex TnpA–RE35 adapted from reference 8 showing the active site and the base pairs between C (TCAA, dark blue) and G (GAAT, light blue). The gray sphere is bound Mn. Right: Two base triplets observed in the TnpA–RE35 complex. (D) Target recognition: single-strand transposon joint (RE–LE junction) and target Ts are presented. For simplicity only the recognition of the target cleavage site is indicated. (E) Cleavage sites recognition in the IS/IS family. Multiple sequence alignment of the cleavage sites and guide sequences using Weblogo (weblogo.berkeley.edu) was carried out on 38, 43 and 23 members of the IS (i), the IS (ii), and the IS (iii) groups, respectively. (F) Linker length distribution of LE and RE from 76 (red) and 80 (blue) different IS, respectively.

Source: microbiolspec July 2015 vol. 3 no. 4 doi:10.1128/microbiolspec.MDNA3-0039-2014
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014.fig4b
FIGURE 4b
Recognition of cleavage sites. Schematic of the canonical and noncanonical base interactions in (A) left end (LE) and (B) right end (RE). The LE and RE are shown in red and blue. Cleavage sequences C or C are placed in black or dark blue boxes; guide sequences G and G are framed in pink and light blue, respectively. Two nucleotides at the 3′ foot of HP involved in triplet formation are highlighted by bold and in black frame. Nucleotide sequences of LE and RE and the base paring within HP and HP are shown. The inset figures describe the interactions between the cleavage sequences and guide sequences. The filled lines indicate canonical base interactions and the dotted lines indicate additional noncanonical base interactions. (C) Structure of the co-complex TnpA–RE35 adapted from reference 8 showing the active site and the base pairs between C (TCAA, dark blue) and G (GAAT, light blue). The gray sphere is bound Mn. Right: Two base triplets observed in the TnpA–RE35 complex. (D) Target recognition: single-strand transposon joint (RE–LE junction) and target Ts are presented. For simplicity only the recognition of the target cleavage site is indicated. (E) Cleavage sites recognition in the IS/IS family. Multiple sequence alignment of the cleavage sites and guide sequences using Weblogo (weblogo.berkeley.edu) was carried out on 38, 43 and 23 members of the IS (i), the IS (ii), and the IS (iii) groups, respectively. (F) Linker length distribution of LE and RE from 76 (red) and 80 (blue) different IS, respectively.
microbiolspec/3/4/MDNA3-0039-2014-fig4b_thmb.gif
microbiolspec/3/4/MDNA3-0039-2014-fig4b.gif
Image of FIGURE 4b

Click to view

FIGURE 4b

Recognition of cleavage sites. Schematic of the canonical and noncanonical base interactions in (A) left end (LE) and (B) right end (RE). The LE and RE are shown in red and blue. Cleavage sequences C or C are placed in black or dark blue boxes; guide sequences G and G are framed in pink and light blue, respectively. Two nucleotides at the 3′ foot of HP involved in triplet formation are highlighted by bold and in black frame. Nucleotide sequences of LE and RE and the base paring within HP and HP are shown. The inset figures describe the interactions between the cleavage sequences and guide sequences. The filled lines indicate canonical base interactions and the dotted lines indicate additional noncanonical base interactions. (C) Structure of the co-complex TnpA–RE35 adapted from reference 8 showing the active site and the base pairs between C (TCAA, dark blue) and G (GAAT, light blue). The gray sphere is bound Mn. Right: Two base triplets observed in the TnpA–RE35 complex. (D) Target recognition: single-strand transposon joint (RE–LE junction) and target Ts are presented. For simplicity only the recognition of the target cleavage site is indicated. (E) Cleavage sites recognition in the IS/IS family. Multiple sequence alignment of the cleavage sites and guide sequences using Weblogo (weblogo.berkeley.edu) was carried out on 38, 43 and 23 members of the IS (i), the IS (ii), and the IS (iii) groups, respectively. (F) Linker length distribution of LE and RE from 76 (red) and 80 (blue) different IS, respectively.

Source: microbiolspec July 2015 vol. 3 no. 4 doi:10.1128/microbiolspec.MDNA3-0039-2014
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014.fig5
FIGURE 5
Strand transfer and reset model of IS transpososome. (A) Inactive form of TnpA dimer in the absence of DNA (pale green, orange ovals and dark green and orange cylinders represent the body and the αD helices of two monomers, respectively). At the ends, dotted red and blue lines represent linkers at left end (LE) and right end (RE), light red and light blue boxes represent G and G, respectively. (B) Binding of a copy of LE and RE resulting in TnpA activation (catalytic sites ). (C) Cleavage of both ends forms a 5′ phosphotyrosine linkage between Y127 and LE on one αD helix (dark orange cylinders) and between Y127 and the RE flank on the other (dark green cylinders). 3′-OH groups are shown as yellow circles. Reciprocal rotation of both αD helices from to configuration are indicated by large arrows. (D) Strand transfer takes place to reconstitute the joined donor backbone (donor joint) and generate the RE–LE transposon junction at configuration. (E) Release of the donor joint and transition from to configuration. (F) Reset to the form and target site engagement. (G) Cleavage of the RE–LE junction and target and transition from to configuration. (H) Regeneration of the left and right transposon ends.
microbiolspec/3/4/MDNA3-0039-2014-fig5_thmb.gif
microbiolspec/3/4/MDNA3-0039-2014-fig5.gif
Image of FIGURE 5

Click to view

FIGURE 5

Strand transfer and reset model of IS transpososome. (A) Inactive form of TnpA dimer in the absence of DNA (pale green, orange ovals and dark green and orange cylinders represent the body and the αD helices of two monomers, respectively). At the ends, dotted red and blue lines represent linkers at left end (LE) and right end (RE), light red and light blue boxes represent G and G, respectively. (B) Binding of a copy of LE and RE resulting in TnpA activation (catalytic sites ). (C) Cleavage of both ends forms a 5′ phosphotyrosine linkage between Y127 and LE on one αD helix (dark orange cylinders) and between Y127 and the RE flank on the other (dark green cylinders). 3′-OH groups are shown as yellow circles. Reciprocal rotation of both αD helices from to configuration are indicated by large arrows. (D) Strand transfer takes place to reconstitute the joined donor backbone (donor joint) and generate the RE–LE transposon junction at configuration. (E) Release of the donor joint and transition from to configuration. (F) Reset to the form and target site engagement. (G) Cleavage of the RE–LE junction and target and transition from to configuration. (H) Regeneration of the left and right transposon ends.

Source: microbiolspec July 2015 vol. 3 no. 4 doi:10.1128/microbiolspec.MDNA3-0039-2014
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014.fig6
FIGURE 6
Transposition of the IS/IS family and the replication fork: “Peel and Paste” transposition mechanism. (A) Excision. Cartoon representing excision of the single-strand circular intermediate (transposon joint) from the lagging strand template of a donor plasmid. Arrow tip represents replication direction. (B) Integration. Integration of right end (RE)–left end (LE) transposon joint into single-strand target at the replication fork.
microbiolspec/3/4/MDNA3-0039-2014-fig6_thmb.gif
microbiolspec/3/4/MDNA3-0039-2014-fig6.gif
Image of FIGURE 6

Click to view

FIGURE 6

Transposition of the IS/IS family and the replication fork: “Peel and Paste” transposition mechanism. (A) Excision. Cartoon representing excision of the single-strand circular intermediate (transposon joint) from the lagging strand template of a donor plasmid. Arrow tip represents replication direction. (B) Integration. Integration of right end (RE)–left end (LE) transposon joint into single-strand target at the replication fork.

Source: microbiolspec July 2015 vol. 3 no. 4 doi:10.1128/microbiolspec.MDNA3-0039-2014
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014.fig7
FIGURE 7a
Y1 transposase domestication. (A) repeated extragenic palindromes (REP), bacterial interspersed mosaic elements (BIME) and REPtron. (i) Representation of two categories of REP structures in / with mismatches in the hairpin stem in orange and light blue, violet box represents the conserved tetranucleotide GTAG. Corresponding iREP structures in red and dark blue where green box represents the complementary tetranucleotide CTAC. (ii) Structure of BIME: REP and iREP separated by linkers C or D. BIME are frequently found as consecutive copies. (iii) Examples of REPtrons from some representative strains. is shown in gray, the flanking genes and in green and in violet, respectively. Arrows represent the direction of transcription. (B) IStron: organization of IStron where Intron and IS parts are indicated. P1–P8 and IGS represents characteristic features of group I Introns. LE, RE, TTGAT target site and two of the IS part are indicated.
microbiolspec/3/4/MDNA3-0039-2014-fig7a_thmb.gif
microbiolspec/3/4/MDNA3-0039-2014-fig7a.gif
Image of FIGURE 7a

Click to view

FIGURE 7a

Y1 transposase domestication. (A) repeated extragenic palindromes (REP), bacterial interspersed mosaic elements (BIME) and REPtron. (i) Representation of two categories of REP structures in / with mismatches in the hairpin stem in orange and light blue, violet box represents the conserved tetranucleotide GTAG. Corresponding iREP structures in red and dark blue where green box represents the complementary tetranucleotide CTAC. (ii) Structure of BIME: REP and iREP separated by linkers C or D. BIME are frequently found as consecutive copies. (iii) Examples of REPtrons from some representative strains. is shown in gray, the flanking genes and in green and in violet, respectively. Arrows represent the direction of transcription. (B) IStron: organization of IStron where Intron and IS parts are indicated. P1–P8 and IGS represents characteristic features of group I Introns. LE, RE, TTGAT target site and two of the IS part are indicated.

Source: microbiolspec July 2015 vol. 3 no. 4 doi:10.1128/microbiolspec.MDNA3-0039-2014
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/microbiolspec/10.1128/microbiolspec.MDNA3-0039-2014.fig7b
FIGURE 7b
Y1 transposase domestication. (A) repeated extragenic palindromes (REP), bacterial interspersed mosaic elements (BIME) and REPtron. (i) Representation of two categories of REP structures in / with mismatches in the hairpin stem in orange and light blue, violet box represents the conserved tetranucleotide GTAG. Corresponding iREP structures in red and dark blue where green box represents the complementary tetranucleotide CTAC. (ii) Structure of BIME: REP and iREP separated by linkers C or D. BIME are frequently found as consecutive copies. (iii) Examples of REPtrons from some representative strains. is shown in gray, the flanking genes and in green and in violet, respectively. Arrows represent the direction of transcription. (B) IStron: organization of IStron where Intron and IS parts are indicated. P1–P8 and IGS represents characteristic features of group I Introns. LE, RE, TTGAT target site and two of the IS part are indicated.
microbiolspec/3/4/MDNA3-0039-2014-fig7b_thmb.gif
microbiolspec/3/4/MDNA3-0039-2014-fig7b.gif
Image of FIGURE 7b

Click to view

FIGURE 7b

Y1 transposase domestication. (A) repeated extragenic palindromes (REP), bacterial interspersed mosaic elements (BIME) and REPtron. (i) Representation of two categories of REP structures in / with mismatches in the hairpin stem in orange and light blue, violet box represents the conserved tetranucleotide GTAG. Corresponding iREP structures in red and dark blue where green box represents the complementary tetranucleotide CTAC. (ii) Structure of BIME: REP and iREP separated by linkers C or D. BIME are frequently found as consecutive copies. (iii) Examples of REPtrons from some representative strains. is shown in gray, the flanking genes and in green and in violet, respectively. Arrows represent the direction of transcription. (B) IStron: organization of IStron where Intron and IS parts are indicated. P1–P8 and IGS represents characteristic features of group I Introns. LE, RE, TTGAT target site and two of the IS part are indicated.

Source: microbiolspec July 2015 vol. 3 no. 4 doi:10.1128/microbiolspec.MDNA3-0039-2014
Permissions and Reprints Request Permissions
Download as Powerpoint

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