Role and regulation of Bacillus subtilis glutamate dehydrogenase genes

Journal of Bacteriology

Volumn 180, Issue 23, 1998, Pages 6298-6305

  Belitsky, Boris R ^a   Sonenshein, Abraham L ^a  

^a TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; GLUTAMATE DEHYDROGENASE; GLUTAMIC ACID; ORNITHINE; PROLINE;

AMINO ACID METABOLISM; ARTICLE; BACILLUS SUBTILIS; BACTERIAL GENE; BACTERIAL GROWTH; BACTERIAL METABOLISM; ENZYME REGULATION; GENE EXPRESSION REGULATION; GENE MUTATION; GENE SEQUENCE; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ANALYSIS;

ANIMALIA; BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); NEGIBACTERIA; PROKARYOTA;

EID: 0031756184     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/.180.23.6298-6305.1998     Document Type: Article

References (50)

1. Altschul, S. F., T. L. Madden, A. A. Schäffer, 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.
2. Anagnastopoulos, C., and J. Spizizen. 1961. Requirements for transformation in Bacillus subtilis. J. Bacteriol. 81:741-746.
3. Baker, P. J., K. L. Britton, P. C. Engel, G. W. Farrants, K. S. Lilley, D. W. Rice, and T. J. Stillman. 1992. Subunit assembly and active site location in the structure of glutamate dehydrogenase. Proteins Struct. Funct. Genet. 12:75-86.
4. Belitsky, B. R. Unpublished data.
5. Belitsky, B. R., and A. L. Sonenshein. 1995. Mutations in GltC that increase Bacillus subtilis gltA expression. J. Bacteriol. 177:5696-5700.
6. Belitsky, B. R., and A. L. Sonenshein. Unpublished data.
7. Belitsky, B. R., M. C. U. Gustafsson, A. L. Sonenshein, and C. von Wachenfeldt. 1997. An lrp-like gene of Bacillus subtilis involved in branched-chain amino acid transport. J. Bacteriol. 179:5448-5457.
8. Belitsky, B. R., P. J. Janssen, and A. L. Sonenshein. 1995. Sites required for regulation of Bacillus subtilis glutamate synthase expression. J. Bacteriol. 177:5686-5695.
9. Bohannon, D. E., and A. L. Sonenshein. 1989. Positive regulation of glutamate biosynthesis in Bacillus subtilis. J. Bacteriol. 171:4718-4727.
10. Burkholder, P. R., and N. H. Giles. 1947. Induced biochemical mutations in Bacillus subtilis. Am. J. Bot. 33:345-348.
11. Calogero, S., R. Gardan, P. Glaser, J. Schweizer, G. Rapoport, and M. Débarbouillé. 1994. RocR, a novel regulatory protein controlling arginine utilization in Bacillus subtilis, belongs to the NtrC/NifA family of transcriptional activators. J. Bacteriol. 176:1234-1241.
12. Cruz-Ramos, H., P. Glaser, L. V. Wray, Jr., and S. H. Fisher. 1997. The Bacillus subtilis ureABC operon. J. Bacteriol. 179:3371-3373.
13. 54 from Gram-negative bacteria. Proc. Natl. Acad. Sci. USA 88:9092-9096.
14. Eggen, R. I. L., A. C. M. Geerling, K. Waldkötter, G. Antranikian, and W. M. de Vos. 1993. The glutamate dehydrogenase-encoding gene of the hyperthermophilic archaeon Pyrococcus furiosus: sequence, transcription and analysis of the deduced amino acid sequence. Gene 132:143-148.
15. Farabaugh, P. J., U. Schmeissner, M. Hofer, and J. H. Miller. 1978. Genetic studies of the lac repressor. VII. On the molecular nature of spontaneous hotspots in the lacI gene of Escherichia coli. J. Mol. Biol. 126:847-863.
16. Fouet, A., and A. L. Sonenshein. 1990. A target for carbon source-dependent negative regulation of the citB promoter of Bacillus subtilis. J. Bacteriol. 172:835-844.
17. Gardan, R., G. Rapoport, and M. Débarbouillé. 1995. Expression of the rocDEF operon involved in arginine catabolism in Bacillus subtilis. J. Mol. Biol. 249:843-856.
18. Gardan, R., G. Rapoport, and M. Débarbouillé. 1997. Role of the transcriptional activator RocR in the arginine-degradation pathway of Bacillus subtilis. Mol. Microbiol. 24:825-837.
19. Glaser, P. Unpublished data.
20. Glaser, P., F. Kunst, M. Arnaud, M.-P. Coudart, W. Gonzales, M.-F. Hullo, M. Ionescu, B. Lubochinsky, L. Marcelino, I. Moszer, E. Presecan, M. Santana, E. Schneider, J. Schwezer, A. Vertes, G. Rapoport, and A. Danchin. 1993. Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325° to 333°. Mol. Microbiol. 10:371-384.
21. Henkin, T. M., F. J. Grundy, W. L. Nicholson, and G. H. Chambliss. 1991. Catabolite repression of α-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacI and galR repressors. Mol. Microbiol. 5:575-584.
22. Hoch, J. A. 1993. spo0 genes, the phosphorelay, and the initiation of sporulation, p. 747-755. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and other gram-positive bacteria: biochemistry, physiology, and molecular genetics. American Society for Microbiology, Washington, D.C.
23. Iijima, T., M. D. Diesterhaft, and E. Freese. 1977. Sodium effect of growth on aspartate and genetic analysis of a Bacillus subtilis mutant with high aspartase activity. J. Bacteriol. 129:1440-1447.
24. Itaya, M. 1992. Construction of a novel tetracycline resistance gene cassette useful as a marker on the Bacillus subtilis chromosome. Biosci. Biotech. Biochem. 56:685-686.
25. Jahns, T. 1992. Occurrence of cold-labile NAD-specific glutamate dehydrogenase in Bacillus species. FEMS Microbiol. Lett. 96:187-192.
26. Janssen, P. J., and J. P. Mueller. Unpublished data.
27. Jourlin, C., A. Bengrine, M. Chippaux, and V. Méjean. 1996. An unorthodox sensor protein (TorS) mediates the induction of the tor structural genes in response to trimethylamine N-oxide in Escherichia coli. Mol. Microbiol. 20:1297-1306.
28. Kane, J. F., J. Wakim, and R. S. Fischer. 1981. Regulation of glutamate dehydrogenase from Bacillus subtilis. J. Bacteriol. 148:1002-1005.
29. Kunst, F., N. Ogasawara, I. Moszer, A. M. Albertini, G. Alloni, V. Azevedo, M. G. Bertero, P. Bessieres, A. Bolotin, S. Borchert, R. Borriss, L. Boursier, A. Brans, M. Braun, S. C. Brignell, S. Bron, S. Brouillet, C. V. Bruschi, B. Caldwell, V. Capuano, N. M. Carter, S. K. Choi, J. J. Codani, I. F. Connerton, N. J. Cummings, R. A. Daniel, F. Denizot, K. M. Devine, A. Dusterhoft, S. D. Ehrlich, P. T. Emmerson, K. D. Entian, J. Errington, C. Fabret, E. Ferrari, D. Foulger, C. Fritz, M. Fujita, Y. Fujita, S. Fuma, A. Galizzi, N. Galleron, S. Y. Ghim, P. Glaser, A. Goffeau, E. J. Golightly, G. Grandi, G. Guiseppi, B. J. Guy, K. Haga, J. Haiech, C. R. Harwood, A. Henaut, H. Hilbert, S. Holsappel, S. Hosono, M. F. Hullo, M. Itaya, L. Jones, B. Joris, D. Karamata, Y. Kasahara, M. Klaerr-Blanchard, C. Klein, Y. Kobayasni, P. Koetter, G. Koningstein, S. Krogh, M. Kumano, K. Kurita, A. Lapidus, S. Lardinois, J. Lauber, V. Lazarevic, S. M. Lee, A. Levine, H. Liu, S. Masuda, C. Mauel, C. Medigue, N. Medina, R. P. Mellado, M. Mizuno, D. Moestl, S. Nakai, M. Noback, D. Noone, M. O'Reilly, K. Ogawa, A. Ogiwara, B. Oudega, S. H. Park, V. Parro, T. M. Pohl, D. Portetelle, S. Porwollik, A. M. Prescott, E. Presecan, P. Pujic, B. Purnelle, G. Rapoport, M. Rey, S. Reynolds, M. Rieger, C. Rivolta, E. Rocha, B. Roche, M. Rose, Y. Sadaie, T. Sato, E. Scanlan, S. Schleich, R. Schroeter, F. Scoffone, J. Sekiguchi, A. Sekowska, S. J. Seror, P. Serror, B. S. Shin, B. Soldo, A. Sorokin, E. Tacconi, T. Takagi, H. Takahashi, K. Takemaru, M. Takeuchi, A. Tamakoshi, T. Tanaka, P. Terpstra, A. Tognoni, V. Tosato, S. Uchiyama, M. Vandenbol, F. Vannier, A. Vassarotti, A. Viari, R. Wambutt, E. Wedler, H. Wedler, T. Weitzenegger, P. Winters, A. Wipat, H. Yamamoto, K. Yamane, K. Yasumoto, K. Yata, K. Yoshida, H. F. Yoshikawa, E. Zumstein, H. Yoshikawa, and A. Danchin. 1997. The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature 390:249-256.
30. Lyerly, D. M., L. A. Barroso, and T. D. Wilkins. 1991. Identification of the latex test-reactive protein of Clostridium difficile as glutamate dehydrogenase. J. Clin. Microbiol. 29:2639-2642.
31. Miller, C. M., S. Baumberg, and P. G. Stockley. 1997. Operator interactions by the Bacillus subtilis arginine repressor/activator, AhrC: novel positioning and DNA-mediated assembly of a transcriptional activator at catabolic sites. Mol. Microbiol. 26:37-48.
32. Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
33. Moran, C. P., Jr. 1993. RNA polymerase and transcription factors, p. 653-667. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and other gram-positive bacteria: biochemistry, physiology, and molecular genetics. American Society for Microbiology, Washington. D.C.
34. Mueller, J. P., G. Bukusoglu, and A. L. Sonenshein. 1992. Transcriptional regulation of Bacillus subtilis glucose starvation-inducible genes: control of gsiA by the ComP-ComA signal transduction system. J. Bacteriol. 174:4361-4373.
35. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
36. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
37. Schreier, H. J. 1993. Biosynthesis of glutamine and glutamate and assimilation of ammonia, p. 281-298. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and other gram-positive bacteria: biochemistry, physiology, and molecular genetics. American Society for Microbiology, Washington, D.C.
38. Schreier, H. J., S. W. Brown, K. D. Hirschi, J. F. Nomellini, and A. L. Sonenshein. 1989. Regulation of Bacillus subtilis glutamine synthetase gene expression by the product of the glnR gene. J. Mol. Biol. 210:51-63.
39. Semon, D., N. R. Movva, T. F. Smith, N. El Alama, and J. Davies. 1987. Plasmid-determined bleomycin resistance in Staphylococcus aureus. Plasmid 17:45-63.
40. Slack, F. J., P. Serror, E. Joyce, and A. L. Sonenshein. 1995. A gene required for nutritional repression of the Bacillus subtilis dipeptide permease operon. Mol. Microbiol. 15:689-702.
41. Smith, E. L., B. M. Austen, K. M. Blumenthal, and J. F. Nyc. 1975. Glutamate dehydrogenases, p. 293-367. In P. D. Boyer (ed.), The enzymes, 3rd ed., vol. XI. Academic Press, New York, N.Y.
42. Sorokin, A., V. Azevedo, E. Zumstein, N. Galleron, S. D. Ehrlich, and P. Serror. 1996. Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome. Microbiology 142:2005-2016.
43. Stillman, T. J., P. J. Baker, K. L. Britton, and D. W. Rice. 1993. Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. J. Mol. Biol. 234:1131-1139.
44. Strauch, M. A. 1993. AbrB, a transition state regulator, p. 757-764. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and other gram-positive bacteria: biochemistry, physiology, and molecular genetics. American Society for Microbiology, Washington, D.C.
45. Sullivan, M. A., R. E. Yasbin, and F. E. Young. 1984. New shuttle vectors for Bacillus subtilis and Escherichia coli which allow rapid detection of inserted fragments. Gene 29:21-26.
46. Teller, J. K., R. J. Smith, M. J. McPherson, P. C. Engel, and J. R. Guest. 1992. The glutamate dehydrogenase gene of Clostridium symbiosum. Cloning by polymerase chain reaction, sequence analysis and overexpression in Escherichia coli. Eur. J. Biochem. 206:151-159.
47. Whatmore, A. M., J. A. Chudek, and R. H. Reed. 1990. The effects of osmotic upshock on the intracellular solute pools of Bacillus subtilis. J. Gen. Microbiol. 136:2527-2535.
48. Wray, L. V., Jr., A. E. Ferson, K. Rohrer, and S. H. Fisher. 1996. TnrA, a transcriptional factor required for global nitrogen regulation in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 93:8841-8845.
49. Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
50. Yip, K. S. P., T. J. Stillman, K. L. Britton, P. J. Artymiuk, P. J. Baker, S. E. Sedelnikova, P. C. Engel, A. Pasquo, R. Chiaraluce, V. Consalvi, R. Scandurra, and D. W. Rice. 1995. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure 3:1147-1158.