1887

Chapter 10 : Transcription Regulation by the Response Regulator Spo0A

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Ebook: Choose a downloadable PDF or ePub file. Chapter is a downloadable PDF file. File must be downloaded within 48 hours of purchase

Buy this Chapter
Digital (?) $15.00

Preview this chapter:
Zoom in
Zoomout

Transcription Regulation by the Response Regulator Spo0A, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555818319/9781555810894_Chap10-1.gif /docserver/preview/fulltext/10.1128/9781555818319/9781555810894_Chap10-2.gif

Abstract:

The ultimate response to the stationary phase varies between species of bacteria, for example, in continued starvation leads to the production of a dormant form, the bacterial endospore. The activity of Spo0A in modulating transcription is affected by its phosphorylation. The purpose of this review is to focus on the mechanism of transcription regulation by Spo0A. The sequencing of the spo0A gene identified that it encoded a member of the response regulator family of proteins. The DNA binding domain was able to repress in vitro transcription from and to activate transcription from the promoter for the operon () in vitro. Recent work on the gp4 protein of the phage φ29 provides an interesting comparison with Spo0ABD. The activation of Spo0A involves phosphorylation of the N terminus of the protein. Mutation of amino acid D56, the site of phosphorylation of Spo0A, demonstrated that it is essential for normal levels of sporulation and for in vitro phosphorylation of the protein by the phosphorelay. The transcription kinetics assays the authors carried out predicted that Spo0A-P stimulated the conversion of an unstable intermediate to one that could initiate RNA synthesis rapidly. The genetic experiments and the in vitro assays lead to the conclusion that the transcription activation functions of Spo0A lie in the C-terminal domain and that these functions are inhibited by the N-terminal domain. The transcription regulation properties of Spo0A are more diverse than have been demonstrated for other response regulators.

Citation: Spiegelman G, Bird T, Voon V. 1995. Transcription Regulation by the Response Regulator Spo0A, p 159-179. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch10

Key Concept Ranking

RNA Polymerase I
0.48783186
Transcription Initiation
0.4495998
Sodium Dodecyl Sulfate
0.43210775
Transcription Start Site
0.4226433
Operon Components
0.40582168
0.48783186
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

Figures

Image of FIGURE 1
FIGURE 1

Amino acid sequence of Spo0A. The amino acid sequence of Spo0A is taken from .Two regions of the amino acid sequence of OmpR are shown where transcription activation mutants (underlined) have been identified ( ). At the C terminus, the amino acid sequence from ϕ29 gp4 and various mutations of the sequence that affect the activity of the protein are shown. The sequence is from and the mutants are from and . Positions of mutations in Spo0A are shown: and mutants are from , mutants that are deletions of the indicated amino acids are from , the coi mutants are from and Δ209, Δ267 mutants are from . The DNA binding motif in Spo0A proposed by Youngman (personal communication) is underlined. Regions marked as helical (α) and extended (β) were calculated using the GGBSM program of PC gene. These regions are not meant to be precise but to allow subdivision of the sequence for discussion. Regions were calculated for the N-terminal and C-terminal domains separately, and so they begin again after the diamond symbol, which indicates the division between the N-terminal and C-terminal domains (as defined in the text). In the C-terminal domain, the positions of the and mutations are indicated (at position 257), and the positions of suppressors of are indicated at H162F () and L174F () ( ).

Citation: Spiegelman G, Bird T, Voon V. 1995. Transcription Regulation by the Response Regulator Spo0A, p 159-179. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch10
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of FIGURE 7
FIGURE 7

Formation of initiation complexes at : stimulation by Spo0A, Spo0A-P, and Spo0ABD. Transcription initiation reactions were composed and analyzed as described in . Reactions contained 100 nM Spo0A-P (closed circles), Spo0ABD (triangles), or Spo0A (open circles), GTP, ATP, and a DNA fragment containing At time zero, RNA polymerase was added to the reaction, and after various incubation times, samples were withdrawn and challenged with a mixture containing CTP, UTP, and heparin. The percentage of template containing an initiated complex is plotted as a function of the time of the initiation reaction assay. The reaction containing Spo0A-P initiated very rapidly, whereas those containing the binding domain showed a pronounced lag, although the final level was only slightly lower than that seen with Spo0A-P.

Citation: Spiegelman G, Bird T, Voon V. 1995. Transcription Regulation by the Response Regulator Spo0A, p 159-179. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch10
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of FIGURE 2
FIGURE 2

0A boxes in regulated promoters. (A) Sequences that have been identified as being protected by Spo0A from digestion by DNase I are indicated in capital letters. In some sequences, the protected regions are not flush on both strands of DNA and unprotected DNA is indicated by lowercase letters. In examples in which both strands are capitals, comparison of the digestion pattern on the two strands has not been performed. The consensus sequence for the 0A box is underlined. The numbering refers to the +1 site for each promoter. (B) Position of the OA boxes relative to the start site of transcription for the promoter is indicated. The symbols indicate forward (>>>>) or reverse (<<<<) orientations. Indicated at the side is the gene or operon where the 0A boxes are located and the σ-factor used by the promoter (σA or σH). Promoters that are activated by Spo0A have an asterisk (*); the other promoters are repressed. The data are taken from ( ), ( ), ( ), ( ), ( ), and ( ).

Citation: Spiegelman G, Bird T, Voon V. 1995. Transcription Regulation by the Response Regulator Spo0A, p 159-179. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch10
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of FIGURE 3
FIGURE 3

Repression of transcription of and promoters by (A) Spo0A-P and (B) Spo0ABD. An 800-bp HindIII-EcoRI fragment from PJM5134 ( ) was excised and filled with the Klenow fragment to create blunt ends. This fragment was used as the template (at 5 nM) in transcription assays composed as described in . The transcription products were separated by electrophoresis through polyacrylamide gels containing 7 M urea and localized and quantitated as described in . The results are presented as the fraction of the extent of transcription in the absence of either Spo0A-P or Spo0ABD. Spo0A-P or Spo0ABD were preincubated with the template at 37°C. RNA polymerase was added, and after 3 min, nucleotides allowing transcript elongation were added. After a 3-min initiation-elongation reaction, heparin was added. This is a multiple round initiation assay. Open symbols are transcripts from ; closed symbols are from .

Citation: Spiegelman G, Bird T, Voon V. 1995. Transcription Regulation by the Response Regulator Spo0A, p 159-179. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch10
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of FIGURE 4
FIGURE 4

Stimulation of transcription from by Spo0A-P and σH. The template used contained cloned adjacent to ribosomal RNA terminators, and the transcription reaction conditions and analysis of product have been described ( ). Core RNA polymerase was incubated with the DNA template, increasing amounts of recombinant σ, either without Spo0A (triangles) or with Spo0A-P (circles). As seen in the presence of Spo0A-P, the stimulation of transcription by low levels of the σ-factor was enhanced. At higher inputs of σ, the increase in transcription was the same in the presence and absence of Spo0A-P. Thus, the presence of Spo0A-P increased the stimulation of transcription by the σ-factor.

Citation: Spiegelman G, Bird T, Voon V. 1995. Transcription Regulation by the Response Regulator Spo0A, p 159-179. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch10
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of FIGURE 5
FIGURE 5

DNase I footprint assay of formation of complexes at . A dIII to PvuII DNA fragment containing ( ) was labeled at the dIII end with [γ-P]ATP and polynucleotide kinase. The fragment was incubated in transcription reaction buffer either alone or in the presence of either Spo0A or Spo0A-P. All reactions contain 0.4 mM ATP, which allows formation of a dinucleotide at . An aliquot of each reaction was removed and treated with 4 µg/ml DNase I for 10 s. The reaction was stopped with 10 mM EDTA, 0.1% sodium dodecyl sulfate. Labeled DNA was recovered by ethanol precipitation, redissolved in formamide gel loading buffer, and electrophoresed on a 6% polyacrylamide gel containing 7 M urea. To examine the rate of complex formation, RNA polymerase (100 nM, final concentration) was added to the template, and after different incubation times, samples were removed and treated with DNase for 10 s as described above. The incubation times (after adding the polymerase) are lane 1,5 s; lane 2, 30 s; lane 3, 1 min; lane 4, 2 min; lane 5, 5 min, lane 6, 15 min. For each set, the lane marked C shows the pattern obtained when no proteins were added, and the lane marked 0 is the pattern obtained before adding RNA polymerase. The nucleotide positions, relative to the transcription initiation site, are given at the left. Without Spo0A or Spo0A-P, a complex between the polymerase and the DNA was formed very rapidly. From our kinetic data, this complex (C) cannot initiate RNA synthesis when challenged with nucleotides and heparin and therefore represents a heparin-sensitive complex. When Spo0A was present, RNA polymerase formed a second type of complex (C), as indicated by the DNase I-hypersensitive sites (arrowheads at the right). This complex also cannot initiate RNA synthesis rapidly when challenged with heparin and thus represents a second heparin-sensitive complex. In the presence of Spo0A-P, a complex (C) formed that lacked one of the sites hypersensitive to DNase I and showed increased protection in the -10 region. This complex cannot complete transcripts when challenged with heparin and nucleotides and so represents a stage before the heparin-resistant complex (HR). The kinetic data suggest that the complex formed in the presence of Spo0A-P (C) can initiate RNA synthesis rapidly. We view the C complex as equivalent to the activated intermediate in the transition to HR complex (Bird et al., unpublished data).

Citation: Spiegelman G, Bird T, Voon V. 1995. Transcription Regulation by the Response Regulator Spo0A, p 159-179. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch10
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of FIGURE 6
FIGURE 6

Reaction mechanism for transcription stimulation at . In the cartoon of initiation, the following symbols are used: double lines represent the DNA template; the large oval represents RNA polymerase; the small circle attached to a small oval represents the two-domain structure of Spo0A. The predicted -10 and —35 consensus sequences at the promoter are indicated on the DNA strands. These sequences are separated by 22 bp instead of the expected 17 to 18 bp. The initial binding of the polymerase and DNA, which is independent of Spo0A, protects only the -35 site of the promoter (C complex). The binding of Spo0A and RNA polymerase to the DNA creates DNase I-hypersensitive sites in the -27, -28 region of the promoter and increased protection near the —10 region (C complex). The DNase I-hypersensitive sites are presumed to result from a distortion of the DNA helix, as represented. The binding of two Spo0A proteins is shown because there are two 0A boxes. Phosphorylation of Spo0A (represented by a change in shading pattern) is presumed to cause a change in the shape of the protein. In the presence of Spo0A-P, C complexes isomerize to C complexes, which are characterized by increased protection of the —10 region and loss of the hypersensitive sites. The change is represented by release of the —35 contacts between the polymerase and the promoter, which were presumed to cause the helix distortion. The release of the —35 contacts allows the polymerase to contact the —10 region. The contacts with the -10 region permit the polymerase in the C complex to synthesize a short RNA (represented by the thick wavy line) on addition of the initiating nucleotides ATP and GTP. The initiated complex is designated HR because it is resistant to the polymerase inhibitor heparin.

Citation: Spiegelman G, Bird T, Voon V. 1995. Transcription Regulation by the Response Regulator Spo0A, p 159-179. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch10
Permissions and Reprints Request Permissions
Download as Powerpoint

References

/content/book/10.1128/9781555818319.chap10
1. Adhya, S.,, and S. Garges. 1990. Positive Control. J. Biol. Chem. 265:1079710800.
2. Aiba, H.,, F. Kakasai,, S. Mizushima,, and T. Mizuno. 1989. Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, results in stimulation of its DNA-binding ability. J. Biochem. 106:57.
3. Austin, S.,, and R. Dixon. 1992. The procaryotic enhancer binding protein NTRC has an ATPase activity which is phosphorylation and DNA dependent. EMBO J. 11:22192228.
4. Baldus, J. M.,, B. D. Green,, P. Youngman,, and C. P. Moran, Jr. 1994. Phosphorylation of Bacillus subtilis transcription factor SpoOA stimulates transcription from the spollG promoter by enhancing binding to weak OA boxes. J. Bacteriol. 176:296306.
5. Barthelemy, I.,, and M. Salas. 1989. Characterization of a new procaryotic transcription activator and its DNA recognition site. J. Mol. Biol. 208:225232.
6. Bird, T.,, D. Burbulys,, J.-J. Wu,, M. A. Strauch, J. A. Hoch,, and G. B. Spiegelman. 1992. The effect of supercoiling on the in vitro transcription of the spollA operon from Bacillus subtilis. Biochemie 74:627634.
7. Bird, T.,, J. Grimsley,, J. A. Hoch,, and G. B. Spiegelman. 1993. Phosphorylation of SpoOA activates its stimulation of in vitro transcription from the Bacillus subtilis spollG operon. Mol. Microbiol. 9:741749.
8. Bird, T.,, and G. B. Spiegelman. Unpublished data.
9. Bird, X.,, J. K. Grimsley,, J. A. Hoch,, and G. B. Spiegelman. Unpublished data.
10. Bowrin, V.,, R. Brissette,, and M. Inouye. 1992.Two transcriptionally active OmpR mutants that do not require phosphorylation by EnvZ in an Escherichia coli cell free system. J. Bacteriol. 174:66856687.
11. Brissette, R. E.,, K. Tsung,, and M. Inouye. 1991. Intramolecular second site revertants to the phosphorylation site mutation in OmpR, a kinase dependent transcriptional activator in Escherchia coli. J. Bacteriol. 173:37493755.
12. Brissette, R. E.,, K. Tsung,, and M. Inouye. 1992. Mutations in a central highly conserved non-DNA binding region of OmpR, an Escherichia coli transcriptional activator, influence its DNA binding ability. J. Bacteriol. 174:49071912.
13. Brown, D. P.,, L. Ganova-Raeva,, B. D. Green,, S. R. Wilkinson,, M. Young,, and P. Youngman. 1994. Characterization of spoOA homologues in diverse Bacillus and Clostridium species identifies a probable DNA-binding domain. Mol. Microbiol. 14:411436.
14. Burbulys, D.,, K. A. Trach,, and J. A. Hoch. 1991. Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay. Cell 64:545552.
15. Chan, B.,, and S. Busby. 1989. Recognition of nucleotide sequences at the Escherichia coli galactose operon PI promoter by RNA polymerase. Gene 84:227236.
16. Chelm, B. K.,, J. J. Duffy,, and E. P. Geiduschek. 1982. Interaction of Bacillus subtilis RNA polymerase core with two specificity determining subunits. Competition between σ and the SP01 gene 28 protein. J. Biol Chem. 257:65016508.
17. Chibazakura, T.,, F. Kawamura,, and T. Takahashi. 1991. Differential regulation of spoOA transcription in Bacillus subtilis: glucose represses promoter switching at the initiation of sporulation. J. Bacteriol. 173:26252632.
18. Choi, S. H.,, and E. P. Greenberg. 1991. The C-terminal region of the Vibrio fisheri LuxR protein contains an inducer independent lux gene activation domain. Proc. Natl. Acad. Sci. USA 88:1111511119.
19. Delgado, J.,, S. Forst,, S. Harlocker,, and M. Inouye. 1993. Identification of a phosphorylation site and functional analysis of conserved aspartic acid residues of OpmR, a transcriptional activator for ompF and ompC in Escherichia coli. Mol. Microbiol. 10:10371047.
20. Dubnau, E.,, J. Weir,, G. Nair,, L. Carter D3,, C. P. Moran, Jr.,, and I. Smith. 1988. Bacillus sporulation gene spoOH codes for σ 30H). J. Bacteriol. 170:10541062.
21. Errington, J. 1993. Bacillus subtilis sporulation: regulation of gene expression and control of morphogenesis. Microbiol. Rev. 57:133.
22. Ferrari, F. A.,, K. Trach,, D. LeCoq,, J. Spence,, E. Ferrari,, and J. A. Hoch. 1985. Characterization of the spoOA locus and its deduced product. Proc. Natl. Acad. Sci. USA 82:26472651.
23. Frantz, B.,, and T. V. O'Halloran. 1990. DNA distortion accompanies transcriptional activation by the metal responsive gene regulatory protein MerR. Biochemistry 29:47474751.
24. Geiduschek, E. P. 1993. Two procaryotic transcriptional enhancer systems. Prog. Nucleic Acids Res. Mol. Biol. 43:109133.
25. Green, B. D.,, M. G. Bramucci,, and P. Youngman. 1991. Mutant forms of SpoOA that affect sporulation initiation: a general model for phosphorylation mediated activation of bacterial signal transduction proteins. Semin. Dev. Biol. 2:2129.
26. Grimsley, J. K.,, R. B. Tjalkens,, M. A. Strauch,, T. H. Bird,, G. B. Spiegelman,, Z. Hostomsky,, J. M. Whiteley,, and J. A. Hoch. 1994. Subunit composition and domain structure of the SpoOA sporulation transcription factor of Bacillus subtilis. J. Biol Chem. 269:1697716982.
27. Hawley, D. K.,, and W. R. McClure. 1982. Mechanism of activation of transcription initiation from the λ PRM promoter. J. Mol. Biol. 157:493525.
28. Hoch, J. A. 1993. Regulation of the phosphorelay and the initiation of sporulation in Bacillus subtilis. Annu. Rev. Microbiol. 74:441466.
29. Hoch, J. A.,, K. Trach,, E. Kawamura,, and H. Saito. 1985. Identification of the transcriptional suppressor sof-1 as an alternation in the SpoOA protein. J. Bacteriol. 161:552555.
30. Huang, K.-J.,, J. L. Schieberl,, and M. M. Igo. 1994. A distant upstream site involved in the negative regulation of the Escherichia coli opmF gene. J. Bacteriol. 176:13091315.
31. Hwang, J.-J.,, S. Brown,, and G. N. Gussin. 1988. Characterization of a doubly mutant derivative of the λ PRM promoter. Effects of mutations on activation of PRM. J. Mol. Biol. 200:695708.
32. Ireton, K.,, D. Z. Rudner,, K. J. Siranosian,, and A. D. Grossman. 1993. Integration of multiple developmental signals in Bacillus subtilis through the SpoOA transcription factor. Genes Dev. 7:283294.
33. Ishihama, A. 1993. Protein-protein communication within the transcription apparatus. J. Bacteriol. 175:24832489.
34. Kahn, D.,, and G. Ditta. 1991. Molecular structure of fixJ: homology of the transcription activator domain with the -35 binding domain of sigma factors. Mol. Microbiol. 5:987997.
35. Kawamura, E.,, and H. Saito. 1983. Isolation and mapping of a new suppressor mutation of an early sporulation gene spoOF mutation in Bacillus subtilis. Mol. Gen. Genet. 192:330334.
36. Kawamura, E.,, L. Wang,, and R. H. Doi. 1985. Catabolite resistant sporulation (crsA) mutations in the Bacillus subtilis RNA polymerase σ 43 gene (rpoD) can suppress and be suppressed by mutations in spo0genes. Proc Natl. Acad. Sci. USA 83:81248128.
37. Keilty, S.,, and M. Rosenberg. 1987. Constitutive function of a positively regulated promoter reveals new sequences essential for activity. J. Biol. Chem. 262:63896395.
38. Kimura, S.,, K. Makino,, H. Shinagawa,, M. Amemura,, and A. Nakata. 1989. Regulation of the phosphate regulon in Escherichia coli: characterization of the promoter of the pstS gene. Mol. Gen. Genet. 215:374380.
39. Kolb, A.,, K. Igarashi,, A. Ishihama,, M. Lavigne,, M. Buckle,, and H. Buc. 1993. E. coli RNA polymerase, deleted in the C-terminal part of its alpha-subunit, interacts differently with the cAMP-CRP complex at the lacVX and at the galPl promoter. Nucleic Acids Res. 21:319326.
40. Kudoh, J.,, T. Dxeuchi,, and K. Kurahashi. 1985. Nucleotide sequence of the sporulation gene spo0A and its mutant genes of Bacillus subtilis. Proc. Natl. Acad. Sci. USA 82:26652668.
41. Kumar, A.,, B. Grimes,, N. Fujita,, K. Makino,, R. A. Malloch,, R. S. Hayward,, and A. Ishihama. 1994. Role of the sigma70 subunit of Escherichia coli RNA polymerase in transcription activation. J. Mol. Biol. 235:405413.
42. Lewandowski, M.,, E. Dubnau,, and I. Smith. 1986. Transcriptional regulation of the spo0F gene of Bacillus subtilis. J. Bacteriol. 168:870877.
43. Li, M.,, M. Moyle,, and M. M. Susskind. 1994. Target of transcriptional activation function of phage λ d protein. Science 263:7577.
44. Losick, R.,, R. Youngman,, and P. J. Piggot. 1986. Genetics of endospore formation in Bacillus subtilis. Annu. Rev. Genet. 20:625669.
45. Makino, K.,, M. Amemura,, S.-K. Kim,, A. Nakata,, and H. Shinagawa. 1993. Role of the a 70 subunit of R N A polymerase in transcriptional activation by activator protein PhoB in Escherichia coli. Genes Dev. 7:149160.
46. Mencia, M.,, M. Salas, and E Rojo. 1993. Residues of the Bacillus subtilis phage ϕ 29 transcriptional activator required both to interact with RNA polymerase and to activate transcription. J. Mol. Biol. 233:695704.
47. Menon, K. P.,, and N. L. Lee. 1990. Activation of ara operon by a truncated AraC protein does not require inducer. Proc. Natl. Acad. Sci. USA 87:37083712.
48. Merrick, M. J. 1993. In a class of its own—the RNA polymerase sigma factor σ 54N). Mol. Microbiol. 10:903909.
49. Meyer, B. J.,, and M. Ptashne. 1980. Gene regulation at the right operator OR of bacteriophage λ . III. λ repressor directly activates gene transcription. J. Mol. Biol. 139:195205.
50. Mizukami, Y.,, T. Sekiya,, and H. Hirokawa. 1986. Nucleotide sequence of gene F of Bacillus phage Nf. Gene 43:231235.
51. Mizuno, T.,, and S. Mizushima. 1990. Signal transduction and gene regulation through the phosphorylation of two regulatory components: the molecular basis for the osmotic regulation of the porin genes. Mol. Microbiol. 4:10771082.
52. Morett, E.,, and L. Segovia. 1993. The a 54 bacterial enhancer binding protein family: mechanism of action and phyolgenetic relationship of their functional domains. J. Bacteriol. 175:60676074.
53. Olmedo, G.,, E. G. Ninfa,, J. Stock,, and P. Youngman. 1990. Novel mutations that alter regulation of sporulation in Bacillus subtilis: evidence that phosphorylation of regulatory protein Spo0A controls the initiation of sporulation. J. Mol. Biol. 215:359372.
54. Parkhill, J.,, A. Z. Axisari,, J. G. Wright,, N. L. Brown,, and T. V. O'Halloran. 1993. Construction and characterization of a mercury-independent MerR activator (MerRAC): transcriptional activation in the absence of Hg(II) is accompanied by DNA distortion. EMBO J. 12:413421.
55. Parkinson, J. S.,, and E. C. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:71112.
56. Perego, M.,, G. B. Spiegelman,, and J. A. Hoch. 1988. Structure of the gene for the transition state regulator, abrB: regulator synthesis is controlled by the spo0A sporulation gene in Bacillus subtilis. Mol. Microbiol. 2:689699.
57. Perego, M.,, J.- J. Wu,, G. B. Spiegelman,, and J. A. Hoch. 1991. Mutational dissociation of the positive and negative regulatory properties of the Spo0A sporulation transcription factor of Bacillus subtilis. Gene 100:207212.
58. Piggot, P. J.,, and J. G. Coote. 1976. Genetic aspects of bacterial endospore formation. Bacteriol. Rev. 40:908962.
59. Porter, S. C.,, A. K. North,, A. B. Wedel,, and S. Kustu. 1993. Ohgomerization of NTRC at the glnA enhancer is required for transcriptional activation. Genes Dev. 7:22582273.
60. Predich, M.,, G. Nair,, and I. Smith. 1992. Bacillus subtilis early sporulation genes kinA, spoOF and spoOA are transcribed by the RNA polymerase containing σ H. J. Bacteriol. 174:27712778.
61. Rampersaud, A.,, S. L. Harlocker,, and M. Inouye. 1994. The OmpR protein of Escherichia coli binds to sites in the ompF promoter region in a hierarchial manner determined by its degree of phosphorylation. J. Biol. Chem. 269:1255912566.
62. Rojo, E.,, A. Zaballos,, and M. Salas. 1990. Bend induced by phage ϕ 29 transcriptional regulator protein p4 in the viral late promoters is required for activation. J. Mol. Biol. 211:713725.
63. w , E. D.,, and T. J. Silhavy. 1992. Alpha the Cinderella subunit of RNA polymerase. J. Biol Chem. 267:1451514518.
64. Russo, E. D.,, J. M. Slauch,, and T. J. Silhavy. 1993. Mutations that affect separate functions of OmpR, the phosphorylated regulator of porin transcription in Escherichia coli. J. Mol. Biol. 231:261273.
65. Sasse-Dwight, S.,, and J. D. Gralla. 1988. Probing the E. coli glnALG upstream activation mechanism in vivo. Proc. Natl. Acad. Sci. USA 85:89348938.
66. Satola, S.,, J. M. Baldus,, and C. P. Moran, Jr. 1992. Binding of Spo0A stimulates spollG promoter activity in Bacillus subtilis. J. Bacteriol. 174:14481453.
67. Satola, S.,, P. A. Kirshman,, and C. P. Moran, Jr. 1991. Spo0A binds to a promoter used by RNA polymerase during sporulation in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 88:45334537.
68. Sharif, T. R.,, and M. M. Igo. 1993. Mutations in the alpha subunit of RNA polymerase that affect regulation of porin gene transcription in Escherichia coli K12. J. Bacteriol. 175:54605468.
69. Sharrock, R. A.,, S. Rubenstein,, M. Chan,, and T. Leighton. 1984. Intergenic suppression of spo0 phenotypes by the Bacillus subtilis mutation rvtA. Mol. Gen. Genet. 194:260264.
70. Shoji, K.,, S. Hiratsuka,, E. Kawamura,, and Y. Kobayashi. 1988. New suppressor mutation sur0B of spo0B and spo0F mutations in Bacillus subtilis. J. Gen. Microbiol. 134:32493257.
71. Slauch, J. M.,, E. D. Russo,, and T. J. Silhavy. 1991. Suppressor mutations in rpoA suggest that OmpR controls transcription by direct interaction with the alpha subunit of RNA polymerase. J. Bacteriol. 173:75017510.
72. Slauch, J. M.,, and T. J. Silhavy. 1991. cis-acting ompF mutations that result in OmpR-dependent constitutive expression. J. Bacteriol. 173:40394048.
73. Sonenshein, A. L.,, J. A. Hoch,, and R. Losick (ed.). 1993. Bacillus subtilis and Other Gram Positive Bacteria. ASM Press, Washington, D. C..
74. Spiegelman, G. B.,, B. Van Hoy,, M. Perego,, J. Day,, K. Trach,, and J. A. Hoch. 1990. Structural alterations in the Bacillus subtilis Spo0A regulatory protein which suppress mutations at several spo0 loci. J. Bacteriol. 172:50115019.
75. Stock, J. B.,, J. A. Ninfa,, and A. M. Stock. 1989. Protein phosphorylation and regulation of adaptive response in bacteria. Microbiol. Rev. 53:450490.
76. Strauch, M. A.,, and J. A. Hoch. 1993. Transition state regulators: sentinels of Bacillus subtilis post exponential gene expression. Mol. Microbiol. 7:337342.
77. Strauch, M. A.,, K. Trach,, J. Day,, and J. A. Hoch. 1992. Spo0A activates and represses its own synthesis by binding at its dual promoters. Biochemie 74:619626.
78. Strauch, M. A.,, V. Webb,, G. B. Spiegelman,, and J. A. Hoch. 1990. The Spo0A protein of Bacillus subtilis is a repressor of the abrB gene. Proc. Natl. Acad. Sci. USA 87:18011805.
79. Strauch, M. A.,, J.-J. Wu,, R. H. Jonas,, and J. A. Hoch. 1993. A positive feedback loop controls transcription of the spo0F gene, a component of the sporulation phosphorelay in Bacillus subtilis. Mol. Microbiol. 7:967974.
80. Trach, K.,, D. Burbulys,, M. A. Strauch,, J.-J. Wu,, N. Dhillion,, R. Jonas,, C. Hanstein,, P. Kallio,, M. Perego,, T. Bird,, G. Spiegelman,, C. Fogher,, and J. A. Hoch. 1991. Control of the initiation of sporulation in Bacillus subtilis by a phosphorelay. Res. Microbiol. 142:815823.
81. Trach, K.,, J. W. Chapman,, P. Piggot,, D. LeCoq,, and J. A. Hoch. 1988. Complete sequence and transcriptional analysis of the spo0F region of the Bacillus subtilis chromosome. J. Bacteriol. 170:41944208.
82. Trach, K.,, J. W. Chapman,, P. J. Piggot,, and J. A. Hoch. 1985. Deduced product of the stage 0 sporulation gene spo0F shares homology with the Spo0A, OmpR and SfrA proteins. Proc. Natl. Acad. Sci. USA 82:72607264.
83. Tsung, K.,, R. E. Brissette,, and M. Inouye. 1989. Identification of the DNA binding domain of the OmpR protein required for transcriptional activation of the ompF and ompC genes of Escherichia coli by in vivo DNA footprinting. J. Biol. Chem. 264:1010410109.
84. Tsung, K.,, R. E. Brissette,, and M. Inouye. 1990. Enhancement of RNA polymerase binding to promoters by a transcriptional activator, OmpR, in Escherichia coli: its positive and negative effects on transcription. Proc. Natl. Acad. Sci. USA 87:59405944.
85. Wanner, B. L. 1993. Gene regulation by phosphate in enteric bacteria. J. Cell. Biochem. 51:4754.
86. Wegrzyn, G.,, R. E. Glass,, and M. S. Thomas. 1992. Involvement of the Escherichia coli RNA polymerase a subunit in transcriptional activation by the bacteriophage lambda CI and CII proteins. Gene 122:17.
87. Weiss, D. S.,, J. Batut,, K. E. Klose,, J. Keener,, and S. Kustu. 1991. The phosphorylated form of the enhancer binding protein NTRC has an ATPase activity that is essential for activation of transcription. Cell 67:155167.
88. West, D.,, R. Williams,, V. Rhodius,, A. Bell,, N. Sharma,, C. Zou,, N. Fujita,, A. Ishihama,, and S. Busby. 1993. Interactions between RNA polymerase cyclic AMP preceptor protein and RNA polymerae at class II promoters. Mol. Microbiol. 10:789797.
89. Whipple, F. W.,, and A. L. Sonenshein. 1992. Mechanism of initiation of transcription by Bacillus subtilis RNA polymerase at several promoters. J. Mol. Biol. 223:399414.
90. Wu, J.-J.,, M. G. Howard,, and P. J. Piggot. 1989. Regulation of transcription of the Bacillus subtilis spoIIA locus. J. Bacteriol. 171:692698.
91. Wu, J.-J.,, P. J. Piggot,, K. M. Tatti,, and C. P. Moran, Jr. 1991. Transcription of the Bacillus subtilis spoIIA locus. Gene 101:113116.
92. Yamashita, S.,, H. Yoshikawa,, F. Kawamura,, H. Takahashi,, T. Yamamoto,, Y. Kobayashi,, and H. Saito. 1986. The effect of spo0 mutations on the expression of spo0A- and spo0F-lacZ fusions. Mol. Gen. Genet. 205:2833.
93. York, K.,, T. J. Kenney,, S. Satola,, C. P. Moran, Jr.,, H. Poth,, and P. Youngman. 1992. Spo0A controls the σ A dependent activation of Bacillus subtilis sporulation specific transcription unit spoIIE. J. Bacteriol. 174:26482658.
94. Zhang, X.,, Y. Zhou,, Y. W. Ebright,, and R. H. Ebright. 1992. Catabolite gene activator protein (CAP) is not an "acidic activating region" transcription activator protein. J. Biol. Chem. 276:81368139.

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