Null Mutation of HvrA Compensates for Loss of an Essential relA/spoT-Like Gene in Rhodobacter capsulatus

Journal of Bacteriology

Volumn 186, Issue 1, 2004, Pages 235-239

  Masuda, Shinji ^a   Bauer, Carl E ^b  

^a RIKEN   (Japan)

^b INDIANA UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN HVRA; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL CHROMOSOME; BACTERIAL GENE; CONTROLLED STUDY; GENE LOSS; GENE MUTATION; LETHALITY; NONHUMAN; NUCLEOTIDE SEQUENCE; NULL ALLELE; PRIORITY JOURNAL; PROMOTER REGION; RELA SPOT LIKE GENE; RHODOBACTER CAPSULATUS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CULTURE MEDIA; GENE EXPRESSION REGULATION, BACTERIAL; GUANOSINE TETRAPHOSPHATE; MOLECULAR SEQUENCE DATA; MUTATION; NF-KAPPA B; PIGMENTS, BIOLOGICAL; PYROPHOSPHATASES; RHODOBACTER CAPSULATUS; TRANS-ACTIVATORS; TRANSCRIPTION FACTOR RELA;

BACTERIA (MICROORGANISMS); PROKARYOTA; RHODOBACTER; RHODOBACTER CAPSULATUS; RHODOPSEUDOMONAS;

EID: 0347622751     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.1.235-239.2004     Document Type: Article

References (30)

1. Aravind, L., and E. V. Koonin. 1998. The HD domain defines a new superfamily of metal dependent phosphohydrolases. Trends Biochem. Sci. 23:469-472.
2. Bauer, C. E., S. Elsen, L. R. Swem, D. L. Swem, and S. Masuda. 2002. Redox and light regulation of gene expression in photosynthetic prokaryotes. Phil. Trans. R. Soc. Lond. B 358:147-154.
3. Bertin, P., N. Benhabiles, E. Krin, C. Laurent-Winter, C. Tendeng, E. Turlin, A. Thomas, A. Danchin, and R. Brasseur. 1999. The structural and functional organization of H-NS-like proteins is evolutionarily conserved in gram-negative bacteria. Mol. Microbiol. 31:319-329.
4. Bochner, B. R., and B. N. Ames. 1982. Complete analysis of cellular nucleotide by two-dimensional thin layer chromatography. J. Biol. Chem. 257:9759-9769.
5. Buggy, J. J., M. W. Sganga, and C. E. Bauer. 1994. Characterization of a light-responding trans-activator responsible for differentially controlling reaction center and light-harvesting-I gene expression in Rhodobacter capsulatus. J. Bacteriol. 176:6936-6943.
6. Cashel, M., D. R. Gentry, V. J. Hernandez, and D. Vinella. 1996. The stringent response, p. 1458-1496. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. 1. ASM Press, Washington, D.C.
7. Chatterji, D., N. Fujita, and A. Ishihama. 1998. The mediator for stringent control, ppGpp, binds to the β-subunit of Escherichia coli RNA polymerase. Genes Cells 3:279-287.
8. Du, S., J.-L. K. Kouadio, and C. E. Bauer. 1999. Regulated expression of a highly conserved regulatory gene cluster is necessary for controlling photosynthesis gene expression in response to anaerobiosis in Rhodobacter capsulatus. J. Bacteriol. 181:4334-4341.
9. Fellay, R., J. Frey, and H. Krisch. 1987. Interposon mutagenesis of soil and water bacteria: a family of DNA fragments designed for in vitro insertional mutagenesis of gram-negative bacteria. Gene 52:147-154
10. Gay, P., D. Le Coq, M. Steinmetz, T. Berkelman, and C. I. Kado. 1985. Positive selection procedure for entrapment of insertion sequence elements in gram-negative bacteria. J. Bacteriol. 164:918-921.
11. Gentry, D. R., and M. Cashel. 1996. Mutational analysis of the Escherichia coli spoT gene identifies distinct but overlapping regions involved in ppGpp synthesis and degradation. Mol. Microbiol. 19:1373-1384.
12. Johansson, J., C. Balsalobre, S. Wang, J. Urbonaviciene, D. J. Jin, B. Sondén, and B. E. Uhlin. 2000. Nucleoid proteins stimulate stringently controlled bacterial promoters: a link between the cAMP-CRP and the (p)ppGpp regulons in Escherichia coli. Cell 102:475-485.
13. Kasai, K., S. Usami, T. Yamada, Y. Endo, K. Ochi, and Y. Tozawa. 2002. A RelA-SpoT homolog (Cr-RSH) identified in Chlamydomonas reinhardtii generates stringent factor in vivo and localizes to chloroplasts in vitro. Nucleic Acids Res. 30:4985-4992.
14. Kern, M., P.-B. Kamp, A. Paschen, B. Masepohl, and W. Klipp. 1998. Evidence for a regulatory link of nitrogen fixation and photosynthesis in Rhodobacter capsulatus via HvrA. J. Bacteriol. 180:1965-1969.
15. Kumar, S., K. Tamura, and M. Nei. 2001. MEGA2: molecular evolutionary genetics analysis software. Bioinformatics 17:1244-1245.
16. Mittenhuber, G. 2001. Comparative genomics and evolution of genes encoding bacterial (p)ppGpp synthetases/hydrolases (the Rel, RelA and SpoT proteins). J. Mol. Microbiol. Biotechnol. 3:585-600.
17. Saitou, N., and M. Nei. 1987. The neighbor-joining methods: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
18. Scolnik, P. A., and B. L. Marrs. 1987. Genetic research with photosynthetic bacteria. Annu. Rev. Microbiol. 41:703-726.
19. Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilizing system for in vivo genetic engineering: transposon mutagenesis in gram-negative bacteria. Bio/Technology 1:784-791.
20. 3 oxidase expression by multiple regulators in Rhodobacter capsulatus. J. Bacteriol. 184:2815-2820.
21. Tedin, K., and H. Bremer. 1992. Toxic effects of high levels of ppGpp in Escherichia coli are relieved by rpoB mutations. J. Biol. Chem. 267:2337-2344.
22. Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
23. Tosa, T., and L. I. Pizer. 1971. Biochemical bases for the antimetabolite action of L-serine hydroxamate. J. Bacteriol. 106:972-982.
24. Toulokhonov, I. I., I. Shulgina, and V. J. Hernandez. 2001. Binding of the transcription effecter ppGpp to Escherichia coli RNA polymerase is allosteric, modular and occurs near the N-terminus of the β-subunit. J. Biol. Chem. 276:1220-1225.
25. van der Biezen, E. A., J. Sun, M. J. Coleman, M. J. Bibb, and J. D. G. Jones. 2000. Arabidopsis RelA/SpoT homologs implicate (p)ppGpp in plant signalling. Proc. Natl. Acad. Sci. USA 97:3747-3752.
26. Weaver, P. F., J. D, Wall, and H. Gest. 1975. Characterization of Rhodopseudomonas capsulata. Arch. Microbiol. 105:207-216.
27. Wendrich, T. M., C. L. Beckering, and M. A. Marahiel. 2000. Characterization of the relA/spoT gene from Bacillus stearothermophilus. FEMS Microbiol. Lett. 190:195-201.
28. Woese, C. R. 1987. Bacterial evolution. Microbiol. Rev. 51:221-271.
29. Xiao, H., M. Kalman, K. Ikehara, S. Zemel, G. Glaser, and M. Cashel. 1991. Residual guanosine 3′, 5′-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations. J. Biol. Chem. 266:5980-5990.
30. Young, D. A., C. E. Bauer, J. C. Williams, and B. L. Marrs. 1989. Genetic evidence for superoperonal organization of genes for photosynthetic pigments and pigment-binding proteins in Rhodobacter capsulatus. Mol. Gen. Genet. 218:1-12.