Characterization of the relA/spoT gene from Bacillus stearothermophilus

FEMS Microbiology Letters

Volumn 190, Issue 2, 2000, Pages 195-201

  Wendrich, Thomas M ^a   Beckering, Carsten L ^a   Marahiel, Mohamed A ^a  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

Bacillus; Guanosine pentaphosphate synthetase; Guanosine 3' diphosphate 5' (tri)diphosphate; RelA; SpoT; Stringent response

Indexed keywords

GUANOSINE 3' DIPHOSPHATE 5' DIPHOSPHATE; GUANOSINE 3' DIPHOSPHATE 5' TRIPHOSPHATE; HYDROLASE; SYNTHETASE;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; ENZYME SYNTHESIS; GENE AMPLIFICATION; GENE LOCUS; GEOBACILLUS STEAROTHERMOPHILUS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; WESTERN BLOTTING;

BACILLUS STEAROTHERMOPHILUS; BACILLUS SUBTILIS; GENE DELETION; GENES, BACTERIAL; GENETIC COMPLEMENTATION TEST; GUANOSINE PENTAPHOSPHATE; LIGASES; MOLECULAR SEQUENCE DATA; PHYLOGENY; PYROPHOSPHATASES; SEQUENCE ANALYSIS, DNA;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); GEOBACILLUS STEAROTHERMOPHILUS; POSIBACTERIA; PROKARYOTA;

EID: 0034666587     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(00)00335-9     Document Type: Article

References (27)

1. Stent G.S., Brenner S. A genetic locus for the regulation of ribonucleic acid synthesis. Proc. Natl. Acad. Sci. USA. 47:1961;2005-2014.
2. Cashel M., Gallant J. Two compounds implicated in the function of the RC Gene of Escherichia coli. Nature. 221:1969;838-841.
3. Cashel, M., Gentry, D.R., Hernandez, V.J. and Vinella, D. (1996) The stringent response. In: Escherichia coli and Salmonella thyphimurium: Cellular and Molecular Biology, vol. 2, Chapter 92 (Neidhardt, F.C. et al., Eds.), pp. 1458-1496. American Society for Microbiology, Washington, DC.
4. Laffler T., Gallant J. spoT, a new genetic locus involved in the stringent response of E. coli. Cell. 1:1974;27-30.
5. Xiao H., Kalman M., Ikehara K., Zemel S., Glaser G., Cashel M. Residual guanosine 3′,5′-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations. J. Biol. Chem. 266:1991;5980-5990.
6. Metzger S., Sarubbi E., Glaser G., Cashel M. Protein sequences encoded by the relA and the spoT genes of Escherichia coli are interrelated. J. Biol. Chem. 264:1989;9122-9125.
7. Fehr S., Richter D. Stringent response of Bacillus stearothermophilus: Evidence for the existence of two distinct guanosine 3′,5′-polyphosphate synthetases. J. Bacteriol. 145:1981;68-73.
8. Avarbock D., Salem J., Li L.S., Wang Z.M., Rubin H. Cloning and characterization of a bifunctional RelA/SpoT homologue from Mycobacterium tuberculosis. Gene. 233:1999;261-269.
9. Chakraburtty R., White J., Takano E., Bibb M. Cloning, characterization and disruption of a (p)ppGpp synthetase gene (relA) of Streptomyces coelicolor A3. Mol. Microbiol. 19:1996;357-368.
10. Mechold U., Malke H. Characterization of the stringent and relaxed responses of Streptococcus equisimilis. J. Bacteriol. 179:1997;2658-2667.
11. Mechold U., Cashel M., Steiner K., Gentry D., Malke H. Functional analysis of a relA/spoT gene homolog from Streptococcus equisimilis. J. Bacteriol. 178:1996;1401-1411.
12. Martinez-Costa O.H., Fernandez-Moreno M.A., Malpartida F. The relA/spoT-homologous gene in Streptomyces coelicolor encodes both ribosome-dependent (p)ppGpp-synthesizing and -degrading activities. J. Bacteriol. 180:1998;4123-4132.
13. Wendrich T.M., Marahiel M.A. Cloning and characterization of a relA/spoT homologue from Bacillus subtilis. Mol. Microbiol. 26:1997;65-79.
14. Wehmeier L., Schafer A., Burkovski A., Kramer R., Mechold U., Malke H., Puhler A., Kalinowski J. The role of the Corynebacterium glutamicum rel gene in (p)ppGpp metabolism. Microbiology. 144:1998;1853-1862.
15. Brown, T.A. (1991) Labfax BIOS Scientific Publisher, Manchester, UK.
16. Miller, J. (1972) A short course in bacterial genetics. A laboratory manual and handbook for Escherichia coli and related bacteria. Cold Spring Harbour Laboratory Press, New York.
17. Harwood, C.R. and Cutting, S.M. (1990) Molecular biological methods in Bacillus subtilis. John Wiley and Sons, Chichester.
18. Spizizen J. Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate. Proc. Natl. Acad. Sci. USA. 44:1958;407-408.
19. Sanger F., Miklen S., Coulson A.R. DNA Sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA. 74:1977;5463-5467.
20. Mechulam Y., et al. Methionyl-tRNA synthetase from Bacillus stearothermophilus: structural and functional identities with the Escherichia coli enzyme. Nucleic Acids Res. 19:1991;3673-3681.
21. Hoch J.A., Mathews J. Chromosomal location of pleiotropic sporulation mutations in Bacillus subtilis. Genetics. 73:1973;215-228.
22. Gonzy-Tréboul G., Karmazyn-Campelli C., Stragier P. Developmental regulation of transcription of the Bacillus subtilis ftsAZ operon. J. Mol. Biol. 224:1992;967-979.
23. Kim L., Mogk A., Schumann W. A xylose-inducible Bacillus subtilis integration vector and its application. Gene. 181:1996;71-76.
24. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature. 227:1970;680-685.
25. Monod, J. (1958) Recherches sur la croissance des cultures bacterienes. Hermann, Paris.
26. Towbin H.T., Stachelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
27. Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.