Prolonged stationary-phase incubation selects for lrp mutations in Escherichia coli K-12

Journal of Bacteriology

Volumn 182, Issue 15, 2000, Pages 4361-4365

  Zinser, Erik R ^a   Kolter, Roberto ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; GLYCINE; HELIX LOOP HELIX PROTEIN; MUTANT PROTEIN; PROTEIN LRP; REGULATOR PROTEIN; SERINE; UNCLASSIFIED DRUG;

ALLELE; AMINO TERMINAL SEQUENCE; ARTICLE; CATABOLISM; CONTROLLED STUDY; ESCHERICHIA COLI K 12; GENE EXPRESSION; GENE FUNCTION; GENE INSERTION; GENE MUTATION; GENETIC ANALYSIS; GENOTYPE; INCUBATION TIME; NATURAL SELECTION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN; REGULATOR GENE; STRAIN DIFFERENCE; TRANSPOSON;

ALANINE; ALLELES; BACTERIAL PROTEINS; CARBON; DNA-BINDING PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; LEUCINE; LEUCINE-RESPONSIVE REGULATORY PROTEIN; MUTATION; PHENOTYPE; SELECTION (GENETICS); SERINE; THREONINE; TIME FACTORS; TRANSCRIPTION FACTORS;

EID: 0033912882     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.15.4361-4365.2000     Document Type: Article

References (44)

1. Åkerlund, T., K. Nordström, and R. Bernander. 1995. Analysis of cell size and DNA content in exponentially growing and stationary-phase hatch cultures of Escherichia coli. J. Bacteriol. 177:6791-6797.
2. Ambartsoumian, G., R. D'Ari, R. T. Lin, and E. B. Newman. 1994. Altered amino acid metabolism in lrp mutants of Escherichia coli K12 and their derivatives. Microbiology 140:1737-1744.
3. Beloin, C., S. Ayora, R. Exley, L. Hirschbein, N. Ogasawara, Y. Kasahara, J. C. Alonso, and L. Hegarat. 1997. Characterization of an lrp-like (lrpC) gene from Bacillus subtilis. Mol. Gen. Genet. 256:63-71.
4. Brennan, R. G., and B. W. Matthews. 1989. The helix-turn-helix DNA hinding motif. J. Biol. Chem. 264:1903-1906.
5. Caetano-Annoles, G. 1993. Amplifying DNA with arbitrary oligonucleotide primers. PCR Methods Appl. 3:85-92.
6. Calvo, J. M., and R. G. Matthews. 1994. The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli. Microbiol. Rev. 58:466-490.
7. Charlier, D., M. Roovers, T.-L. Thia-Toong, V. Durbecq, and N. Glansdorff. 1997. Cloning and identification of the Sulfolobus solfataricus lrp gene encoding an archaeal homologue of the eubactcrial leucine-responsive global transcriptional regulator Lrp. Gene 201:63-68.
8. Connell, N., Z. Han, F. Moreno, and R. Kolter. 1987. An E. coli promoter induced by the cessation of growth. Mol. Microbiol. 1:195-201.
9. Cui, Y., M. A. Midkiff, Q. Wang, and J. M. Calvo. 1996. The leucine-responsive regulatory protein (Lrp) from Escherichia coli. J. Biol. Chem. 271:6611-6617.
10. Ernsting, B. R., J. W. Denninger, R. M. Blumenthal, and R. G. Matthews. 1993. Regulation of the gltBDF operon of Escherichia coli: how is a leucine-insensitive operon regulated by the leucine-responsive regulatory protein? J. Bacteriol. 175:7160-7169.
11. Finkel, S. E., and R. Kolter. 1999. Evolution of microbial diversity during prolonged starvation. Proc. Natl. Acad. Sci. USA 96:4023-4027.
12. Finkel, S. E., E. Zinser, S. Gupta, and R. Kolter. 1997. Life and death in stationary phase, p. 3-16. In S. J. W. Busby, C. M. Thomas, and N. L. Brown (ed.), Molecular microbiology. Springer-Verlag, Berlin, Germany.
13. Fix, D. F., P. A. Burns, and B. W. Glickman. 1987. DNA sequence analysis of spontaneous mutation in a PolA1 strain of Escherichia coli indicates sequence-specific effects. Mol. Gen. Genet. 207:267-272.
14. Friedberg, D., J. V. Platko, B. Tyler, and J. M. Calvo. 1995. The amino acid sequence of Lrp is highly conserved in four enteric microorganisms. J. Bacteriol. 177:1624-1626.
15. Gupta, S. 1997. Mutations that confer a competitive advantage during starvation. M.A. thesis. Harvard University, Cambridge, Mass.
16. Harrison, S. C., and A. K. Aggarwal. 1990. DNA recognition by proteins with the helix-turn-helix motif. Annu. Rev. Biochem. 59:933-969.
17. Hochschild, A., N. Irwin, and M. Ptashne. 1983. Repressor structure and the mechanism of positive control. Cell 32:319-325.
18. Isenberg, S., and E. B. Newman. 1974. Studies on L-serine deaminase in Escherichia coli K-12. J. Bacteriol. 118:53-58.
19. Jankovic, M., T. Kostic, and D. J. Savic. 1990. DNA sequence analysis of spontaneous hislidine mutations in a polA1 strain of Escherichia coli K12 suggests a specific role of the GTGG sequence. Mol. Gen. Genet. 223:481-486.
20. Jordan, S. J., C. E. R. Dodd, and G. S. A. B. Stewart. 1999. Use of single-strand conformation polymorphism analysis to examine the variability of the rpoS sequence in environmental isolates of salmonellae. Appl. Environ. Microbiol. 65:3582-3587.
21. King, N. D., and M. R. O'Brian. 1997. Identitication of the lrp gene in Bratlyrhizonium japonicum and its role in regulation of δ-aminolevulinic acid uptake. J. Bacteriol. 179:1828-1831.
22. Kleckner, N. 1989. Transposon Tn10, p. 227-268. In D. E. Berg and M. M. Howe (ed.), Mobile DNA. ASM Press, Washington, D.C.
23. Kleckner, N., J. Bender, and S. Gottesman. 1991. Uses of transposons with emphasis on Tn10. Methods Enzymol. 204:139-180.
24. Kyrpides, N. C., and C. A. Ouzounis. 1995. The eubacterial transcription activator Lrp is present in the archaeon Pyrococcus furiousus. Trends Biochem. Sci. 20:140-141.
25. Landgraf, J. R., J. Wu, and J. M. Calvo. 1996. Effects of nutrition and growth rate on Lrp levels in Escherichia coli. J. Bacteriol. 178:6930-6936.
26. Lin, R., R. D'Ari, and E. B. Newman. 1990. The leueinc regulon of Escherichia coli K-12: a mutation in rblA alters expression of L-leucine-dependent metabolic opcrons. J. Bacteriol. 172:4529-4535.
27. Martinez, E., B. Bartolome, and F. De la Cruz. 1988. pACYC184-derived cloning vectors containing the multiple cloning site and lacZα reporter gene of pUC8/9 and pUC18/19 plasmids. Gene 68:159-162.
28. Mathew, E., J. Zhi, and M. Freundlich. 1996. Lrp is a direct repressor of the dad operon in Escherichia coli. J. Bacteriol. 178:7234-7240.
29. Miller, J. H. 1992. A short course in bacterial genetics. Cold Spring Harbor Press, Cold Spring Harbor, N.Y.
30. Mondragón, A., S. Subbiah, S. C. Almo, M. Drottar, and S. C. Harrison. 1989. Structure of the amino-terminal domain of phage 434 repressor at 2.0 A resolution. J. Mol. Biol. 205:189-200.
31. Morita, R. V. 1988. Bioavailability of energy and its relationship to growth and starvation survival in nature. Can. J. Microbiol. 34:436-441.
32. Morita, R. V. 1993. Bioavailability of energy and the starvation state, p. 1-23. In S. Kjelleberg (ed.), Starvation in bacteria. Plenum Press, New York, N.Y.
33. Newman, E. B., R. T. Lin, and R. D'Ari. 1996. The leucine/Lrp regulon, p. 1513-1525. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schacchter, and H. E. Umbarger (ed.), Eicherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, D.C.
34. Platko, J. V., and J. M. Calvo. 1993. Mutations affecting the ability of Escherichia coli Lrp to bind DNA, activate transcription, or respond to leucine. J. Bacteriol. 175:1110-1117.
35. Siegele, D. A., and R. Kolter. 1993. Isolation and characterization of an Escherichia coli mutant defective in resuming growth after starvation. Genes Dev. 7:2629-2640.
36. Singer, M., T. A. Baker, G. Schnitzler, S. M. Deischel, M. Goel, W. Dove, K. J. Jaacks, A. D. Grossman, J. W. Erickson, and C. A. Gross. 1989. A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli. Microbiol. Rev. 53:1-24.
37. Su, H., B. F. Lang, and E. B. Newman. 1989. L-Serine degradation in Escherichia coli K-12: cloning and sequencing of the sdaA gene. J. Bacteriol. 171:5095-51112.
38. Waterman, S. R., and P. L. C. Small. 1996. Characterization of the acid resistance phenotype and rpoS alleles of Shiga-like toxin-producing Escherichia coli. Infect. Immun. 64:2808-2811.
39. Wild, J., and B. Obrepalska. 1982. Regulation of expression of the dadA gene encoding D-amino acid dehydrogenase in Escherichia coli: analysis of dadA-lac fusions and direction of dadA transcription. Mol. Gen. Genet. 186:405-410.
40. Willins, D. A., C. W. Ryan, J. V. Platko, and J. M. Calvo. 1991. Characterization of Lrp, an Escherichia colt regulatory protein that mediates a global response to leucine. J. Biol. Chem. 266:10768-10774.
41. Zambrano, M. M., and R. Kolter. 1993. Escherichia coli mutants lacking NADH dehydrogenase-I have a competitive disadvantage in stationary phase. J. Bacteriol. 175:5642-5647.
42. Zambrano, M. M., and R. Kolter. 1996. GASPing for life in stationary phase. Cell 86:181-184.
43. Zambrano, M. M., D. A. Siegele, M. Almirón, A. Tormo, and R. Kolter. 1993. Microbial competition: Escherichia coli mutants that take over stationary phase cultures. Science 259:1757-1760.
44. Zinser, E. R., and R. Kolter. 1999. Mutations enhancing amino acid catabolism confer a growth advantage in stationary phase. J. Bacteriol. 181:5800-5807.