Mutations that increase expression of the rpoS gene and decrease its dependence on hfq function in Salmonella typhimurium

Journal of Bacteriology

Volumn 179, Issue 3, 1997, Pages 656-662

  Brown, Larissa ^a   Elliott, Thomas ^a  

^a WEST VIRGINIA UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BACTERIOPHAGE; BINDING SITE; DNA SEQUENCE; GENE EXPRESSION; GENE MUTATION; GENETIC ANALYSIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN SECONDARY STRUCTURE; SALMONELLA TYPHIMURIUM;

EID: 0031015418     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.3.656-662.1997     Document Type: Article

References (68)

1. Archer, C. D., J. Jin, and T. Elliott. 1996. Stabilization of a HemA-LacZ hybrid protein against proteolysis during carbon starvation in atp mutants of Salmonella typhimurium. J. Bacteriol. 178:2462-2464.
2. S-dependent genes in Escherichia coli. J. Bacteriol. 177:3455-3464.
3. Brown, L., and T. Elliott. 1996. Efficient translation of the RpoS sigma factor in Salmonella typhimurium requires host factor I, an RNA-binding protein encoded by the hfq gene. J. Bacteriol. 178:3763-3770.
4. Brown, L., and T. Elliott. Unpublished observations.
5. Carmichael, G. G., K. Weber, A. Niveleau, and A. J. Wahba. 1975. The host factor required for RNA phage Qβ replication in vitro. Intracellular location, quantitation, and purification by polyadenylate-cellulose chromatography. J. Biol. Chem. 250:3607-3612.
6. Carter-Muenchau, P., and R. E. Wolf, Jr. 1989. Growth-rate-dependent regulation of 6-phosphogluconate dehydrogenase level mediated by an anti Shine-Dalgarno sequence located within the Escherichia coli gnd structural gene. Proc. Natl. Acad. Sci. USA 86:1138-1142.
7. Cheng, S.-W. C., E. C. Lynch, K. R. Leason, D. L. Court, B. A. Shapiro, and D. L. Friedman. 1991. Functional importance of sequence in the stem-loop of a transcription terminator. Science 254:1205-1207.
8. Court, D. L. 1993. RNA processing and degradation by RNase III, p. 71-116. In J. Belasco and G. Brawerman (ed.), Control of messenger RNA stability. Academic Press, Inc., New York, N.Y.
9. 8a. Crick, F. H. C. 1966. Codon-anticodon pairing: the wobble hypothesis. J. Mol. Biol. 19:548-555.
10. Davis, R. W., D. Botstein, and J. R. Ruth. 1980. Advanced bacterial genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
11. de Smit, M. H., and J. van Duin. 1990. Control of prokaryotic translational initiation by mRNA secondary structure. Prog. Nucleic Acid Res. Mol. Biol. 38:1-35.
12. de Smit, M. H., and J. van Duin. 1990. Secondary structure of the ribosome binding site determines translational efficiency: a quantitative analysis. Proc. Natl. Acad. Sci. USA 87:7668-7672.
13. de Smit, M. H., and J. van Duin. 1994. Translational initiation on structured messengers. Another role for the Shine-Dalgarno interaction. J. Mol. Biol. 235:173-184.
14. Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
15. Elliott, T. 1989. Cloning, genetic characterization, and nucleotide sequence of the hemA-prfA operon of Salmonella typhimurium. J. Bacteriol. 171:3948-3960.
16. Elliott, T. 1992. A method for constructing single-copy lac fusions in Salmonella typhimurium and its application to the hemA-prfA operon. J. Bacteriol. 174:245-253.
17. Fang, F. C., S. J. Libby, N. A. Buchmeier, P. C. Loewen, J. Switala, J. Harwood, and D. G. Guiney. 1992. The alternative σ factor KatF (RpoS) regulates Salmonella virulence. Proc. Natl. Acad. Sci. USA 89:11978-11982.
18. Fiers, W. 1975. Chemical structure and biological activity of bacteriophage MS2 RNA, p. 353-396. In N. Zinder (ed.), RNA phages. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
19. Fox, G. E., and C. R. Woese. 1975. 5S RNA secondary structure. Nature 256:505-507.
20. Franze de Fernandez, M. T., L. Eoyang, and J. T. August. 1968. Factor fraction required for the synthesis of bacteriophage Qβ RNA. Nature 219:588-590.
21. Franze de Fernandez, M. T., W. S. Hayward, and J. T. August. 1972. Bacterial proteins required for replication of phage Qβ ribonucleic acid. Purification and properties of Host Factor I, a ribonucleic acid-binding protein. J. Biol. Chem. 247:824-831.
22. Fukumi, H., and K. Imahori. 1971. Control of translation by the conformation of messenger RNA. Proc. Natl. Acad. Sci. USA 68:570-573.
23. Gay, N. J. 1984. Construction and characterization of an Escherichia coli strain with a uncI mutation. J. Bacteriol. 158:820-825.
24. S is positively regulated by ppGpp. J. Bacteriol. 175:7982-7989.
25. Gold, L. M. 1988. Posttranscriptional regulatory mechanisms in Escherichia coli. Annu. Rev. Biochem. 57:199-233.
26. Hall, M. N., J. Gabay, M. Debarbouille, and M. Schwartz. 1982. A role for mRNA secondary structure in the control of translation initiation. Nature 295:610-618.
27. Hengge-Aronis, R. 1993. Survival of hunger and stress: the role of rpoS in early stationary phase gene regulation in E. coli. Cell 72:165-168.
28. Hengge-Aronis, R., R. Lange, N. Henneberg, and D. Fischer. 1993. Osmotic regulation of rpoS-dependent genes in Escherichia coli. J. Bacteriol. 175:259-265.
29. Herlitze, S., and M. Koenen. 1990. A general and rapid mutagenesis method using polymerase chain reaction. Gene 91:143-147.
30. Hong, J.-S., and B. N. Ames. 1971. Localized mutagenesis of any specific small region of the bacterial chromosome. Proc. Natl. Acad. Sci. USA 68: 3158-3162.
31. Kajitani, M., and A. Ishihama. 1991. Identification and sequence determination of the host factor gene for bacteriophage Qβ. Nucleic Acids Res. 19:1063-1066.
32. Kajitani, M., A. Kato, A. Wada, Y. Inokuchi, and A. Ishihama. 1994. Regulation of the Escherichia coli hfq gene encoding the host factor for phage Qβ. J. Bacteriol. 176:531-534.
33. Krinke, L., and D. L. Wulff. 1990. The cleavage specificity of RNase III. Nucleic Acids Res. 18:4809-4815.
34. S subunit of RNA polymerase in Escherichia coli. J. Bacteriol. 177:4676-4680.
35. S subunit of RNA polymerase in Escherichia coli is controlled at levels of transcription, translation and protein stability. Genes Dev. 8:1600-1612.
36. Lodish, H. F. 1970. Secondary structure of bacteriophage f2 ribonucleic acid and the initiation of in vitro protein biosynthesis. J. Mol. Biol. 50:689-702.
37. Lodish, H. F. 1975. Regulation of in vitro protein synthesis by bacteriophage RNA by RNA tertiary structure, p. 301-318. In N. Zinder (ed.), RNA phages. Cold Spring Harbor Laboratory. Cold Spring Harbor, N.Y.
38. S (KatF) in bacterial global regulation. Annu. Rev. Microbiol. 48:53-80.
39. Lynn, S. P., L. M. Kasper, and J. F. Gardner. 1988. Contributions of RNA secondary structure and length of the thymidine tract to transcription termination at the thr operon attenuator. J. Biol. Chem. 263:472-479.
40. Ma, C. K., T. Kolesnikow, J. C. Rayner, E. L. Simons, H. Yim, and R. W. Simons. 1994. Control of translation by mRNA secondary structure: the importance of the kinetics of structure formation. Mol. Microbiol. 14:1033-1047.
41. Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
42. Montañez, C., J. Bueno, U. Schmeissner, D. L. Court, and G. Guarneros. 1986. Mutations of bacteriophage lambda that define independent but overlapping RNA processing and transcription termination sites. J. Mol. Biol. 191:29-37.
43. S subunit of RNA polymerase in Escherichia coli. EMBO J. 15:1333-1339.
44. Muffler, A., D. Fischer, and R. Hengge-Aronis. 1996. The RNA-binding protein HF-I, known as a host factor for phage Qβ RNA replication, is essential for rpoS translation in Escherichia coli. Genes Dev. 10:1143-1151.
45. Mulvey, M. R., and P. C. Loewen. 1989. Nucleotide sequence of katF of Escherichia coli suggests KatF protein is a novel σ transcription factor Nucleic Acids Res. 17:9979-9991.
46. Nakao, H., H. Watanabe, S.-I. Nakayama, and T. Takeda. 1995. yst gene expression in Yersinia enterocolitica is positively regulated by a chromosomal region that is highly homologous to Escherichia coli host factor 1 gene (hfq). Mol. Microbiol. 18:859-865.
47. Nguyen, L. H., D. B. Jensen, N. E. Thompson, D. R. Gentry, and R. R. Burgess. 1993. In vitro functional characterization of overproduced Escherichia coli katF/rpoS gene product. Biochemistry 32:11112-11117.
48. Petersen, C. 1989. Long-range translational coupling in the rplJL-rpoBC operon of Escherichia coli. J. Mol. Biol. 206:323-332.
49. Pratt, L. A., and T. J. Silhavy. 1996. The response regulatory SprE controls the stability of RpoS. Proc. Natl. Acad. Sci. USA 93:2488-2492.
50. Saito, H., and C. C. Richardson. 1981. Processing of mRNA by ribonuclease III regulates expression of gene 1.2 of bacteriophage T7. Cell 27:533-542.
51. Schmieger, H. 1972. Phage P22 mutants with increased or decreased transductional abilities. Mol. Gen. Genet. 119:75-88.
52. Schultz, V. P., and W. S. Reznikoff. 1990. In vitro secondary structure analysis of mRNA from lacZ translation initiation mutants. J. Mol. Biol. 211:427-445.
53. S) by ClpXP protease. J. Bacteriol. 178:470-476.
54. Senear, A. W., and J. A. Steitz. 1976. Site-specific interaction of Qβ host factor and ribosomal protein S1 with Qβ and R17 bacteriophage RNAs. J. Biol. Chem. 251:1902-1912.
55. 53a. Shine, J., and L. Dalgarno. 1974. The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 71:1342-1346.
56. Silhavy, T. J., M. L. Berman, and L. W. Enquist. 1984. Experiments with gene fusions. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
57. Simons, R. W. 1988. Naturally occurring antisense RNA control - a brief review. Gene 72:35-44.
58. Simons, R. W., F. Houman, and N. Kleckner. 1987. Improved single and multicopy lac-based cloning vectors for protein and operon fusion. Gene 53:85-96.
59. Steitz, J. A. 1975. Ribosome recognition of initiator regions in the RNA bacteriophage genome, p. 319-352. In N. Zinder (ed.). RNA phages. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
60. Swords, E., and W. Benjamin. Personal communication.
61. 38, is a second principal σ factor of RNA polymerase in stationary-phase Escherichia coli. Proc. Natl. Acad. Sci. USA 90:3511-3515.
62. Tsui, H.-C. T., H.-C. E. Leung, and M. E. Winkler. 1994. Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12. Mol. Microbiol. 13:35-49.
63. Vieira, J., and J. Messing. 1987. Production of single-stranded plasmid DNA. Methods Enzymol. 153:3-11.
64. Wong, R. Y.-P., and M. M. Susskind. Personal communication.
65. Wulczyn, F. G., and R. Kahmann. 1991. Translational stimulation: RNA sequence and structure requirements for binding of Com protein. Cell 65:259-269.
66. Wulff, D. L., M. Mahoney, A. Shatzman, and M. Rosenberg. 1984. Mutational analysis of a regulatory region in bacteriophage 1 that has overlapping signals for the initiation of transcription and translation. Proc. Natl. Acad. Sci. USA 81:555-559.
67. S, in Escherichia coli: involvement of the nucleoid protein H-NS. EMBO J. 14:594-602.
68. Yura, T., H. Nagai, and H. Mori. 1993. Regulation of the heat-shock response in bacteria. Annu. Rev. Microbiol. 47:321-350.