Control of spoT-dependent ppGpp synthesis and degradation in Escherichia coli

Journal of Molecular Biology

Volumn 259, Issue 1, 1996, Pages 41-57

  Murray, K Daniel ^a   Bremer, Hans ^a  

^a UNIVERSITY OF TEXAS AT DALLAS   (United States)

Author keywords

E. coli; ppGpp; spoT

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; BACTERIAL RNA; GUANOSINE 3' DIPHOSPHATE 5' DIPHOSPHATE; HYDROLASE; MESSENGER RNA; SODIUM AZIDE; SYNTHETASE; TRANSFER RNA;

ARTICLE; BACTERIAL GENE; BACTERIAL GROWTH; BACTERIUM CULTURE; CULTURE MEDIUM; ENZYME REGULATION; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE METABOLISM; PRIORITY JOURNAL; PROTEIN SYNTHESIS; RNA TRANSLATION; TRANSCRIPTION REGULATION;

EID: 0029943235     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0300     Document Type: Article

References (58)

1. An, G., Justesen, J., Watson, R. J. & Friesen, J. D. (1979). Cloning the spoT gene of Escherichia coli: identification of the spoT gene product. J. Bacteriol. 137, 1100-1110.
2. Bremer, H. & Dennis, P. P. (1987). Modulation of chemical composition and other parameters of the cell by growth rate. In Escherichia coli and Salmonella typhimurium, Part IV. Growth of Cells and Cultures (Neidhardt et al., eds), pp. 1527-1542, American Society for Microbiology Washington DC.
3. Bremer, H. & Ehrenberg, M. (1995). Guanosine tetraphosphate as a global regulator of bacterial RNA synthesis: a model involving RNA polymerase pausing and queueing. Biochim. Biophys. Acta, 1262, 15-36.
4. Brunschede, H. & Bremer, H. (1971). Synthesis and breakdown of proteins in Escherichia coli during amino acid starvation. J. Mol. Biol. 57, 35-57.
5. Brunschede, H., Dove, T. & Bremer, H. (1977). Establishment of exponential growth after a nutritional shift-up in Escherichia coli B/r: accumulation of deoxyribonucleic acid, ribonucleic acid and protein. J. Bacteriol. 129, 1020-1033.
6. Cashel, M. (1969). The control of ribonucleic acid synthesis in Escherichia coli: IV. Relevance of unusual phosphorylated compounds from amino acid-starved stringent strains. J. Biol. Chem. 244, 3133-3141.
7. Cashel, M. & Rudd, K. E. (1987). The stringent response. In Escherichia coli and Salmonella typhimurium (Neidhardt et al., eds), vol. 2, pp. 1410-1438, American Society for Microbiology Washington DC.
8. Cole, J. R., Olson, C. L., Hershey J. W. B., Grunberg-Manago, M. & Nomura, M. (1987). Feedback regulation of rRNA synthesis in Escherichia coli: requirement for initiation factor IF2. J. Mol. Biol. 198, 383-392.
9. De Boer, H. A., Bakker, A. J., Weyer, W. J. & Gruber, M. (1976). The role of energy-generating processes in the degradation of guanosine tetraphosphate, ppGpp, in Escherichia coli. Biochim. Biophys. Acta, 432, 361-368.
10. Fehr, S. & Richter, D. (1981). Stringent response of Bacillus stearothermophilus: evidence for the existence of two distinct guanosine 3′,5′-polyphosphate synthetases. J. Bacteriol. 145, 68-73.
11. Fehr, S., Godt, F., Isono, K. & Richter, D. (1979). A ribosome-independent stringent factor from Bacillus stearothermophilus and a low molecular weight substance inhibitory to its activity FEBS Letters, 97, 91-95.
12. Fiil, N. P., Willumsen, B. M., Friesen, J. D. & von Meyenburg, K. (1977). Interaction af alleles of the relA, relC, and spoT genes in Escherichia coli: analysis of the interconversion of GTP, ppGpp, and pppGpp. Mol. Gen. Genet. 150, 87-101.
13. Friesen, J., Fiil, N., Parker, J. M. & Haseltine, W. A. (1974). A new relaxed mutant of Escherichia coli with an altered 50 S ribosomal subunit. Proc. Natl Acad. Sci. USA, 71, 3465-3469.
14. Friesen, J., Fiil, N. & von Meyenburg, K. (1975). Synthesis and turnover of basal level guanosine tetraphosphate in Escherichia coli. J. Biol. Chem. 250, 304-309.
15. Gallant, J., Margason, G. & Finch, B. (1972). On the turnover of ppGpp in Escherichia coli. J. Biol. Chem. 247, 6055-6058.
16. Gentry D. & Cashel, M. (1995). Cellular location of the Escherichia coli SpoT protein. J. Bacteriol. 177, 3890-3893.
17. Hamming, J., Ab, G. & Gruber, M. (1980). E. coli RNA polymerase-rRNA promoter interactions and the effect of ppGpp. Nucl. Acids Res. 8, 3947-3963.
18. Hansen, M., Pato, M., Fiil, N. & von Meyenburg, K. (1975). Simple downshift and resulting lack of correlation between ppGpp pool size and ribonucleic acid accumulation. J. Bacteriol. 122, 585-591.
19. Harshman, R. B. & Yamazaki, H. (1971). Formation of ppGpp in a relaxed and stringent strain of Escherichia coli during diauxic lag. Biochemistry, 10, 3980-3982.
20. Haseltine, W. & Block, R. (1973). Synthesis of guanosine tetra- and pentaphosphate requires the presence of a codon-specific, uncharged transfer ribonucleic acid in the acceptor sites of ribosomes. Proc. Natl Acad. Sci. USA, 70, 1564-1568.
21. Haseltine, W., Block, R., Gilbert, W. & Weber, K. (1972). MSI and MSII made on ribosome on idling step of protein synthesis. Nature, 238, 381-384.
22. Heinemeyer, E. A. & Richter, D. (1977). In vitro degradation of guanosine tetraphosphate (ppGpp) by an enzyme associated with the ribosomal fraction from Escherichia coli. FEBS Letters, 84, 357-361.
23. Heinemeyer, E. A. & Richter, D. (1978). Mechanism of the in vitro breakdown of guanosine 5′-diphosphate 3′-diphosphate in Escherichia coli. Proc. Natl Acad. Sci. USA, 75, 4180-4183.
24. Helmstetter, C. (1967). Rate of DNA synthesis during the division cycle of Escherichia coli B/r. J. Mol. Biol. 24, 417-427.
25. Hernandez, V. J. & Bremer, H. (1990). Guanosine tetraphosphate (ppGpp) dependence of the growth rate control of rrnB P1 promoter activity in Escherichia coli. J. Biol. Chem. 265, 11605-11614.
26. Hernandez, V. J. & Bremer, H. (1991). Escherichia coli ppGpp synthetase II activity requires spoT. J. Biol. Chem. 266, 5991-5999.
27. Hernandez, V. J. & Bremer, H. (1993). Characterization of Escherichia coli devoid of ppGpp. J. Biol. Chem. 268, 10851-10862.
28. Jensen, K. F. & Pedersen, S. (1990). Metabolic growth rate control in Escherichia coli may be a consequence of subsaturation of the macromolecular biosynthetic apparatus with substrates and catalytic components. Microbiol. Rev. 54, 89-100.
29. Johnson, G. S., Adler, C. R., Collins, J. J. & Court, D. (1979). Role of the spoT gene product and manganese ion in the metabolism of guanosine 5′-diphosphate 3′-diphosphate in Escherichia coli. J. Biol. Chem. 254, 5483-5487.
30. Kingston, R., Gutell, R., Taylor A. & Chamberlin, M. (1981). Transcriptional mapping of plasmid pKK3535: quantitation of the effect of guanosine tetraphosphate on binding to the rrnB promoters and a promoter with sequence homologies to the CII binding region. J. Mol. Biol. 146, 433-449.
31. Kjeldgaard, N. O., Maaloe, O. & Schaechter, M. (1958). The transition between different physiological states during balances growth of Salmonella typhimurium. J. Gen. Microbiol. 19, 607-616.
32. Kurland, C. G. & Maaloe, O. (1962). Regulation of ribosomal and transfer RNA synthesis. J. Mol. Biol. 4, 193-210.
33. Laffler, T. & Gallant, J. (1974). SpoT, a new genetic locus involved in the stringent response in E. coli. Cell, 1, 27-30.
34. Lagosky, P. & Chang, F. (1980). Influence of amino acid starvation on guanosine 5′-diphosphate, 3′-diphosphate basal level synthesis in Escherichia coli. J. Bacteriol. 144, 499-508.
35. Lazzarini, R., Cashel M. & Gallant, J. (1971). On the regulation of guanosine tetraphosphate levels in stringent and relaxed strains of Escherichia coli. J. Biol. Chem. 246, 4381-4385.
36. Little, R. & Bremer, H. (1982). Quantitation of guanosine 5′,3′-bisdiphosphate in extracts from bacterial cells by ion-pair reverse-phase high-performance liquid chromatography Anal. Biochem. 126, 381-388.
37. Little, R., Ryals J. & Bremer, H. (1983a). rpoB mutation in Escherichia coli alters control of ribosome synthesis by guanosine tetraphosphate. J. Bacteriol. 154, 787-792.
38. Little, R., Ryals J. & Bremer, H. (1983b). Physiological characterization of Escherichia coli rpoB mutants with abnormal control of ribosome synthesis. J. Bacteriol. 155, 1162-1170.
39. Metzger, S., Sarubbi, E., Glaser, G. & Cashel, M. (1989). Protein sequences encoded by the relA and the spoT genes of Escherichia coli are interrelated. J. Biol. Chem. 264, 9122-9125.
40. Pedersen, F. S., Lund, E. & Kjelgaard, N. O. (1973). Codon specific, tRNA-dependent in vitro synthesis of ppGpp and pppGpp. Nature New Biol. 243, 13-15.
41. Reddy P. S., Raghavan, A. & Chatterji, D. (1995). Evidence for ppGpp binding site on E. coli RNA polymerase: proximity relationship with the rifampicin binding domain. Mol. Microbiol. 15, 255-265.
42. Richter, D. (1979). In vitro synthesis and decay of guanosine 3′,5′-bis(diphosphate) [ppGpp]. In Ribosomes (Chambliss, G., Craven, G. R., Davis, J., Davis, K., Kahan, L., & Nomura, M., eds), pp. 743-765, University Park Press, Baltimore, MD.
43. Richter, D. (1980). Uncharged tRNA inhibits guanosine 3′,5′-bis(diphosphate)3′-pyrophosphohydrolase [ppGppase], the spoT gene product, from Escherichia coli. Mol. Gen. Genet. 178, 325-327.
44. Richter, D., Fehr S. & Harder, R. (1979). The guanosine 3′,5′-bis(diphosphate) (ppGpp) cycle. Eur. J. Biochem. 99, 57-64.
45. Ryals, J., Little, R. & Bremer, H. (1982). Control of rRNA and tRNA syntheses in Escherichia coli by guanosine tetraphosphate. J. Bacteriol. 151, 1261-1268.
46. Sarubbi, E., Rudd, K. E., Xiao, H., Ikehara, K., Kalman, M. & Cashel, M. (1989). Characterization of the spoT gene of Escherichia coli. J. Biol. Chem. 264, 15074-15082.
47. Shen, V. & Bremer, H. (1977). Chloramphenicol-induced changes the synthesis of ribosomal, transfer and messenger ribonucleic acid in Escherichia coli B/r. J. Bacteriol. 130, 1098-1108.
48. Silhavy T. J., Berman, M. L. & Enquist, L. W. (1984). Experiments with Gene Fusions. pp. 107-112, Cold Spring Harbor Laboratory Cold Spring Harbor, NY.
49. Singer, M., Baker, T. A., Schnitzler, G., Deischel, S. M., Goel, M., Dove, W., Jaacks, K. J., Grossman, A. D., Erikson, J. W. & Gross, C. A. (1989). A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli. Microbiol. Rev. 53, 1-24.
50. Stent, G. & Brenner, S. (1961). A genetic locus for the regulation of RNA synthesis. Proc. Natl Acad. Sci. USA, 47, 2005-2014.
51. Sy, J. (1976). A ribosome-independent, soluble stringent factor-like enzyme isolated from a Bacillus brevis. Biochemistry, 15, 606-609.
52. Sy, J. (1977). In vitro degradation of guanosine 5′-diphosphate, 3′-diphosphate. Proc. Natl Acad. Sci. USA, 74, 5529-5533.
53. Sy, J. (1979). Biosynthesis of guanosine tetraphosphate in Bacillus brevis. In Regulation of Macromolecular Synthesis by Low Molecular Weight Mediators (Koch, G. & Richter, D., eds), pp. 94-106, Academic Press, New York.
54. Sy, J. & Akers, H. (1976). Purification and properties of guanosine 5′,3′-polyphosphate synthetase from Bacillus brevis. Biochemistry, 15, 4399-4403.
55. Tedin, K. & Bremer, H. (1992). Toxic effects of high levels of ppGpp in Escherichia coli are relieved by rpoB mutations. J. Biol. Chem. 267, 2337-2344.
56. Xiao, H., Kalman, M., Ikehara, K., Zemel, S., Glaser, G. & Cashel, M. (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.
57. Yegian, C. D., Stent, G. S. & Martin, E. M. (1966). Intracellular condition of Escherichia coli transfer RNA. Proc. Natl. Acad. Sci. USA, 55, 839-846.
58. Zhang, X. & Bremer, H. (1995). Control of the Escherichia coli rrnB P1 promoter strength by ppGpp. J. Biol. Chem. 270, 11181-11189.