The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells

Journal of Bacteriology

Volumn 184, Issue 22, 2002, Pages 6109-6114

  Gaidenko, Tatiana A ^a   Kim, Tae Jong ^a   Price, Chester W ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR G; PHOSPHATASE; PHOSPHOTRANSFERASE; PRION PROTEIN; PRKC KINASE; SERINE THREONINE PHOSPHATASE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; CELL DENSITY; CELL VIABILITY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; NONHUMAN; PLEIOTROPY; PRIORITY JOURNAL; PROTEIN TARGETING;

BACILLUS SUBTILIS; POSIBACTERIA;

EID: 0036842045     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.184.22.6109-6114.2002     Document Type: Article

References (26)

1. Alper, S., A. Dufour, D. A. Garsin, L. Duncan, and R. Losick. 1996. Role of adenosine nucleotides in the regulation of a stress-response transcription factor in Bacillus subtilis. J. Mol. Biol. 260:165-177.
2. Altschul, S. F., T. L. Madden, A. A. Schaffer, J. Zhang, Z. Zhang, W. Miller, and D. J. Lipman. 1997. Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res. 25:3389-3402.
3. Anagnostopulos, C., and J. Spizizen. 1961. Requirements for transformation in Bacillus subtilis. J. Bacteriol. 81:741-746.
4. Antelmann, H., J. Bernhardt, R. Schmid, H. Mach, U. Völker, and M. Hecker. 1997. First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis. Electrophoresis 18:1451-1463.
5. B transcription factor of Bacillus subtilis. J. Bacteriol. 175:7931-7937.
6. B by a regulatory pathway responsive to stationary-phase signals. J. Bacteriol. 174:3695-3706.
7. Dufour, A., and W. G. Haldenwang. 1994. Interactions between a Bacillus subtilis anti-sigma factor (RsbW) and its antagonist (RsbV). J. Bacteriol. 176:1813-1820.
8. Duncan, L., S. Alper, F. Arigoni, R. Losick, and P. Stragier. 1995. Activation of cell-specific transcription by a serine phosphatase at the site of asymmetric division. Science 270:641-644.
9. F from Bacillus subtilis. Proc. Natl. Acad. Sci. USA 90:2325-2329.
10. Gaidenko, T. A., X. Yang, Y. M. Lee, and C. W. Price. 1999. Threonine phosphorylation of modulator protein RsbR governs its ability to regulate a serine kinase in the environmental stress signaling pathway of Bacillus subtilis. J. Mol. Biol. 288:29-39.
11. Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
12. Kunst, F., N. Ogasawara, I. Moszer, A. M. Albertini, G. Alloni, et al. 1997. The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature 390:249-256.
13. Leighton, T. J., and R. H. Doi. 1971. The stability of messenger ribonucleic acid during sporulation in Bacillus subtilis. J. Biol. Chem. 252:268-272.
14. Miller, J. H. 1972. Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
15. F, the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-σ factor that is also a protein kinase. Cell 74:735-742.
16. Mitchell, C., P. W. Morris, and J. C. Vary. 1992. Identification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis. J. Bacteriol. 174:2474-2477.
17. Nairn, A., and H. C. Palfrey. 1996. Regulation of protein synthesis by calcium, p. 295-318. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational Control. Cold Spring Harbor Laboratory Press. Plainview, N.Y.
18. Obuchowski, M., E. Madec, D. Delattre, G. Boël, A. Iwanicki, D. Foulger, and S. J. Séror. 2000. Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family. J. Bacteriol. 182:5634-5638.
19. Price, C. W. 2001. General stress response, p. 369-384. In A. L. Sonenshein, R. Losick, and J. A. Hoch (ed.), Bacillus Subtilis and its Closest Relatives: From Genes to Cells. American Society for Microbiology, Washington, D.C.
20. Robertson, E. S., L. A. Aggison, and A. W. Nicholson. 1994. Phosphorylation of elongation factor G and ribosomal protein S6 in bacteriophage T7-infected Escherichia coli. Mol. Microbiol. 11:1045-1057.
21. Shevchenko, A., M. Wilm, and M. Mann. 1996. Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels. Anal. Chem. 68:850-858.
22. Shi, L., M. Potts, and P. J. Kennelly. 1998. The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases of prokaryotic organisms: A family portrait. FEMS Microbiol. Rev. 22:229-253.
23. Stahl, M. L., and E. Ferrari. 1984. Replacement of the Bacillus subtilis subtilisin structural gene with an in vitro-derived deletion mutation. J. Bacteriol. 158:411-418.
24. Tatusov, R. L., D. A, Natale, I. V. Garkavtsev, T. A. Tatusova, U. T. Shankavaram, B. S. Rao, B. Kiryutin, M. Y. Galperin, N. D. Fedorova, and E. V. Koonin. 2001. The COG database: New developments in phylogenetic classification of proteins from complete genomes. Nucleic Acids Res. 29:22-28.
25. B transcription factor of Bacillus subtilis. Mol. Microbiol. 35:180-188.
26. Yang, X., C. M. Kang, M. S. Brody, and C. W. Price. 1996. Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor. Genes Dev. 10:2265-2275.