Reversion rates in a leuB auxotroph of Escherichia coli K-12 correlate with ppGpp levels during exponential growth

Microbiology

Volumn 143, Issue 3, 1997, Pages 847-854

  Wright, Barbara E ^a   Minnick, Michael F ^a  

^a UNIVERSITY OF MONTANA   (United States)

Author keywords

Mutation rates; ppGpp; Starvation; Stringent response

Indexed keywords

LEUCINE; METHIONINE; SERINE; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; AUXOTROPHY; BACTERIAL GROWTH; ESCHERICHIA COLI; MOLECULAR CLONING; NONHUMAN; NUCLEIC ACID BASE SUBSTITUTION; PRIORITY JOURNAL; REVERTANT;

EID: 0030974929     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-143-3-847     Document Type: Article

References (43)

1. Ames, B. N. & Garry, B. (1959). Coordinate repression of the synthesis of four histidine biosynthetic enzymes by histidine. Proc Natl Acad Sci USA 45, 1453-1461.
2. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. & Strahl, K. (1989). Short Protocols in Molecular Biology. New York: John Wiley & Sons.
3. Blasi, F. & Bruni, C. B. (1981). Regulation of the histidine operon: translation-controlled transcription termination (a mechanism in common to several biosynthetic operons). Curr Top Cell Regul 19, 1-45.
4. Burns, R. O., Calvo, J., Margolin, P. & Umbarger, H. E. (1966). Expression of the leu operon. J Bacteriol 91, 1570-1576.
5. Cashel, M. & Rudd, K. E. (1987). The stringent response. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, pp. 1410-1438. Edited by F. C. Neidhardt, J. L. Ingraham, K. Brooks Low, B. Magasanik, M. Schaechter & H. E. Umbarger. Washington DC: American Society for Microbiology.
6. Chung, C. T., Niemela, S. L. & Miller, R. H. (1985). One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc Natl Acad Sci USA 86, 2172-2175.
7. Cordaro, J. C. & Balbinder, E. (1967). An operator constitutive mutation in a mutant for the first structural gene of the tryptophane operon. Bacteriol Proc 15, 51.
8. Datta, A. & Jinks-Robertson, S. (1995). Association of increased spontaneous mutation rates with high levels of transcription in yeast. Science 268, 1616-1619.
9. Davis, B. D. (1989). Transcriptional bias: a non-Lamarkian mechanism for substrate-induced mutations. Proc Natl Acad Sci USA 96, 5005-5009.
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. Fiil, N. P., Meyenburg, K. V. & Friesen, J. D. (1972). Accumulation and turnover of guanosine tetraphosphate in Escherichia coli. J Mol Biol 71, 769-783.
12. Fitch, F. W. (1982). The challenges to Darwinism since the last centennial and the impact of molecular studies. Evolution 36, 1133-1143.
13. Friesen, J. D., Fiil, N. P. & von Meyenburg, K. (1975). Synthesis and turnover of basal level guanosine tetraphosphate in Escherichia coli. J Biol Chem 250, 304-309.
14. Gallant, J., Margason, G. & Finch, B. (1972). On the turnover of ppGpp in Escherichia coli. J Biol Chem 247, 6055-6058.
15. Hanawalt, P. & Mellan, I. (1993). Stranded in an active gene. Curr Biol 3, 67-69.
16. Herman, R. K. & Dworkin, N. B. (1971). Effect of gene induction on the rate of mutagenesis by ICR-191 in Escherichia coli. J Bacteriol 106, 543-550.
17. Kirino, H., Aoki, M., Aoshima, M., Hayashi, Y., Ohba, M., Yamagishi, A., Wakagi, T. & Oshima, T. (1994). Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus. Eur J Biochem 220, 275-281.
18. Lagosky, P. A. & Chang, F. N. (1980). Influence of amino acid starvation on guanosine 5′-diphosphate 3′-diphosphate basal-level synthesis in Escherichia coli. J Bacteriol 144, 499-508.
19. Lazzarini, R. A., 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.
20. Lea, D. E. & Coulson, C. A. (1949). The distribution of the number of mutants in bacterial populations. J Genet 49, 264-285.
21. Lindahl, T. & Nyberg, B. (1972). Rate of depurination of native deoxyribonucleic acid. Biochemistry 11, 3610-3618.
22. Lindahl, T. & Nyberg, B. (1974). Heat-induced deamination of cytosine residues in deoxyribonucleic acid. Biochemistry 13, 3405-3410.
23. Luria, S. & Delbrück, M. (1943). Mutations of bacteria from virus sensitivity to virus resistance. Genetics 28, 491-504.
24. Metzgar, S., Schreiber, G., Alzenman, E., Cashel, M. & Glaser, G. (1989). Characterization of the relA1 mutation and a comparison of relA1 with new relA null alleles in Escherichia coli. J Biol Chem 264, 21146-21152.
25. Riggs, D. L., Mueller, R. D., Kwan, H.-S. & Artz, S. W. (1986). Promoter domain mediates guanosine tetraphosphate activation of the his operon. Proc Natl Acad Sci USA 83, 9333-9337.
26. Rudd, K. E., Bochner, B. R., Cashel, M. & Roth, J. R. (1985). Mutations in the spoT gene of Salmonella typhimurium: effects on his gene expression. J Bacteriol 163, 534-542.
27. Ryan, F. J. (1955). Spontaneous mutation in non-dividing bacteria. Genetics 40, 726-738.
28. Sambrook, J. E., Fritsch, E. F. & Maniatis, T. (1989). Molecular Cloning: a Laboratory Manual, 2nd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
29. Sarubbi, E., Rudd, K. E. & Cashel, M. (1988). Basal ppGpp level adjustment shown by new spoT mutants affects steady state growth rates and rrnA ribosomal promoter regulation in Escherichia coli. Mol Gen Genet 213, 214-222.
30. Savić, D. J. & Kanazir, D. T. (1972). The effect of a histidine operator - constitutive mutation on UV induced mutability with the histidine operon of Salmonella typhimurium. Mol Gen Genet 118, 45-50.
31. Selby, C. P. & Sancar, A. (1994). Mechanisms of transcription-repair coupling and mutation frequency decline. Microbiol Rev 58, 317-329.
32. Shand, R. F., Blum, P. H., Mueller, R. D., Riggs, D. L. & Artz, S. W. (1989). Correlation between histidine operon expression and guanosine 5′-diphosphate-3′-diphosphate levels during amino acid downshift in stringent and relaxed strains of Salmonella typhimurium. J Bacteriol 171, 737-743.
33. Siebenlist, U., Simpson, R. B. & Gilbert, W. (1980). E. coli RNA polymerase interacts homologously with two different promoters. Cell 20, 269-281.
34. Singer, B. & Kusmierek, J. T. (1982). Chemical mutagenesis. Annu Rev Biochem 52, 655-693.
35. Stephens, J. C., Artz, S.W. & Ames, B. N. (1975). Guanosine 5′-diphosphate (ppGpp): positive effector for histidine operon transcription and general signal for amino-acid deficiency. Proc Natl Acad Sci USA 72, 4389-4393.
36. Stewart, F. M., Gordon, D. M. & Levin, B. R. (1990). Fluctuation analysis: the probability distribution of the number of mutants under different conditions. Genetics 124, 175-185.
37. Tracy, T. E. & Mulcahy, L. S. (1991). A simple method for direct automated sequencing of PCR fragments. BioTechniques 11, 68-75.
38. Winkler, M. E., Roth, D. J. & Hartman, P. E. (1978). Promoter- and attenuator-related metabolic regulation of the Salmonella typhimurium histidine operon. J Bacteriol 133, 830-843.
39. Winkler, M. E., Zawodny, R. V. & Hartman, P. E. (1979). Mutation spoT of Escherichia coli increases expression of the histidine operon deleted for the attenuator. J Bacteriol 139, 993-1000.
40. Wright, B. E. (1996). The effect of the stringent response on mutation rates in E. coli K12. Mol Microbiol 19, 213-219.
41. Wright, B. E. (1997). Does selective gene activation direct evolution? FEBS Lett (in press).
42. 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.
43. Yanisch-Perron, C., Vieira, J. & Messing, J. (1985). Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-119.