Accumulation of ppGpp in Streptococcus pyogenes and Streptococcus rattus following amino acid starvation

FEMS Microbiology Letters

Volumn 159, Issue 1, 1998, Pages 21-26

  Whitehead, Kathryn E ^a   Webber, Gillian M ^a   England, Reg R ^a  

^a UNIVERSITY OF CENTRAL LANCASHIRE   (United Kingdom)

Author keywords

ppGpp; RelA; SpoT; Streptococcus; Stringent response

Indexed keywords

GUANOSINE 3' DIPHOSPHATE 5' DIPHOSPHATE;

ARTICLE; CELL FRACTIONATION; CONTROLLED STUDY; EXTRACT; GENE EXPRESSION REGULATION; IMMUNOBLOTTING; NONHUMAN; PRIORITY JOURNAL; PROTEIN MALNUTRITION; STARVATION; STREPTOCOCCUS; STREPTOCOCCUS PYOGENES;

AMINO ACIDS; ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; BLOTTING, WESTERN; CELL FRACTIONATION; CULTURE MEDIA; GENE EXPRESSION REGULATION, BACTERIAL; GUANOSINE TETRAPHOSPHATE; KINETICS; MUPIROCIN; STREPTOCOCCUS MUTANS; STREPTOCOCCUS PYOGENES;

POSIBACTERIA; RATTUS; STREPTOCOCCUS; STREPTOCOCCUS PYOGENES; STREPTOCOCCUS RATTI;

EID: 0032007680     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(97)00537-5     Document Type: Article

References (19)

1. Cashel, M., Gentry, D.R., Hernandez, V.J. and Vinella, D. (1996) The stringent response. In: Escherichia coli and Salmonella: Cellular and Molecular Biology (Neidhardt, F.C. et al., Eds.), pp. 1458-1496. American Society for Microbiology, Washington, DC.
2. Gentry, D. and Cashel, M. (1993) Cellular localization of the Escherichia coli SpoT protein. J. Bacteriol. 177, 3890-3893.
3. Xiao, H., Kalman, M. Glaser, G., Ikehara, K. Glaser, G. and Cashel, M. (1991) Residual guanosine 3′,5′-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutants. J. Biol. Chem. 266, 5980-5990.
4. Chiaverotti, T.A., Parker, G., Gallant, J. and Agabian, A. (1981) Conditions that trigger guanosine tetraphosphate accumulation in Caulobacter crescentus. J. Bacteriol. 145, 1463-1465.
5. Spadaro, A., Spena, A., Santonastaso, V. and Donini, P. (1981) Stringency without ppGpp accumulation. Nature 291, 256-258.
6. Belitsky, B. and Kari, C. (1982) Absence of Accumulation of ppGpp and RNA during Amino Acid Starvation in Rhizobium meliloti. J. Biol. Chem. 257, 4677-4679.
7. Acosta, R. and Lueking, D.R. (1987) Stringency in the absence of ppGpp accumulation in Rhodobacter sphaeroides. J. Bacteriol. 169, 908-912.
8. McDowell, T.D., Reed, K.E. and Hadley, W.M. (1988) Accumulation of ppGpp in three streptococci during periods of amino acid starvation. FEMS Microbiol. Lett. 56, 151-156.
9. Jones, C., Thompson, A. and England, R.R. (1996) Guanosine 5′-diphosphate 3′-diphosphate (ppGpp), guanosine 5′-diphosphate 3′-monophosphate (ppGp) and antibiotic production in Streptomyces clavuligerus. Microbiology UK, 142, 1789-1795.
10. Mechold, U., Cashel, M., Steiner, K., Gentry, D. and Malke, H. (1996) Functional analysis of a relA/spoT homolog from Streptococcus equisimilis J. Bacteriol. 178, 1401-1411.
11. Mechold, U. and Malke, H. (1997) Characterization of the stringent and relaxed responses of Streptococcus equisimilis. J. Bacteriol. 179, 2658-2667.
12. Haseltine, W.A., Block, R., Gilbert, W. and Weber, K. (1972) MS1 and MSII made on ribosome in idling step of protein synthesis. Nature 238, 381-384.
13. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle or protein-dye binding. Anal. Biochem. 72, 248-254.
14. Hughes, J. and Mellows, G. (1978) Inhibition of isoleucyl-transfer ribonucleic acid synthetase in Escherichia coli by pseudomonic acid. Biochem. J. 176, 305-318.
15. van de Rijn, I. and Kessler, R.E. (1980) Growth characteristics of group A streptococci in a new chemically defined medium. Infect. Immun. 27, 444-448.
16. Pedersen, F.S. and Kjeldgaard, N.O. (1977) Analysis of the relA gene product of E. coli. Eur. J. Biochem. 76, 91-97.
17. Cochran, J.W. and Byrne, R. W. (1974) Isolation and properties of a ribosome-bound factor required for ppGpp and pppGpp synthesis in Escherichia coli. J. Biol. Chem. 249, 353-360.
18. Sy, J. (1976) A ribosome-independent, soluble stringent factor-like enzyme isolated from a Bacillus brevis. Biochemistry 15, 606-609.
19. Block, R. and Haseltine, W.A. (1975) Purification and properties of stringent factor. J. Biol. Chem. 250, 1212-1217.