Escherichia coli rpoS gene has an internal secondary translation initiation region

Biochemical and Biophysical Research Communications

Volumn 313, Issue 2, 2004, Pages 294-299

  Subbarayan, Pochi Ramalingam ^a,b,c   Sarkar, Malancha ^c  

^a NATIONAL INSTITUTE OF GENETICS   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^c UNIVERSITY OF MIAMI MILLER SCHOOL OF MEDICINE   (United States)

Author keywords

Amber mutants; GASP mutants; Internal translation initiation; rpoSAm; STIR; 1 53 s; s; 38

Indexed keywords

AMBER; MUTANT PROTEIN; RNA POLYMERASE; RNA POLYMERASE SIGMA SUBUNIT; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CODON; DOWNSTREAM PROCESSING; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE FUNCTION; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE ANALYSIS; TRANSCRIPTION INITIATION SITE; TRANSLATION INITIATION;

ESCHERICHIA COLI;

EID: 0345735301     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.11.132     Document Type: Article

References (39)

1. Helmann J.D., Chamberlin M.J. Structure and function of bacterial sigma factors. Annu. Rev. Biochem. 57:1988;839-872.
2. Lonetto M., Gribskov M., Gross C.A. The sigma 70 family: sequence conservation and evolutionary relationships. J. Bacteriol. 174:1992;3843-3849.
3. Mulvey M.R., Loewen P.C. Nucleotide sequence of katF of Escherichia coli suggests KatF protein is a novel sigma transcription factor. Nucleic Acids Res. 17:1989;9979-9991.
4. Tanaka K., Takayanagi Y., Fujita N., Ishihama A., Takahashi H. Heterogeneity of the principal sigma factor in Escherichia coli: the rpoS gene product, sigma 38, is a second principal sigma factor of RNA polymerase in stationary-phase Escherichia coli. Proc. Natl. Acad. Sci. USA. 90:1993;8303.
5. Ishihama A. Functional modulation of Escherichia coli RNA polymerase. Annu. Rev. Microbiol. 54:2000;499-518.
6. Lange R., Hengge-Aronis R. Identification of a central regulator of stationary-phase gene expression in Escherichia coli. Mol. Microbiol. 5:1991;49-59.
7. McCann M.P., Kidwell J.P., Matin A. The putative sigma factor KatF has a central role in development of starvation-mediated general resistance in Escherichia coli. J. Bacteriol. 173:1991;4188-4194.
8. Dombroski A.J., Walter W.A., Gross C.A. Amino-terminal amino acids modulate sigma-factor DNA-binding activity. Genes Dev. 7:1993;2446-2455.
9. Wilson C., Dombroski A.J. Region 1 of sigma 70 is required for efficient isomerization and initiation of transcription by Escherichia coli RNA polymerase. J. Mol. Biol. 267:1997;60-74.
10. Sharp M.M., Chan C.L., Lu C.Z., Marr M.T., Nechaev S., Merritt E.W., Severinov K., Roberts J.W., Gross C.A. The interface of sigma with core RNA polymerase is extensive, conserved, and functionally specialized. Genes Dev. 13:1999;3015-3026.
11. Rajkumari K., Gowrishankar J. An N-terminally truncated RpoS (sigma(S)) protein in Escherichia coli is active in vivo and exhibits normal environmental regulation even in the absence of rpoS transcriptional and translational control signals. J. Bacteriol. 184:2002;3167-3175.
12. Gowrishankar J., Yamamoto K., Subbarayan P.R., Ishihama A. In vitro properties of RpoS (sigma(S)) mutants of Escherichia coli with postulated N-terminal subregion 1.1 or C-terminal region 4 deleted. J. Bacteriol. 185:2003;2673-2679.
13. Ohnuma M., Fujita N., Ishihama A., Tanaka K., Takahashi H. A carboxy-terminal 16-amino-acid region of sigma(38) of Escherichia coli is important for transcription under high-salt conditions and sigma activities in vivo. J. Bacteriol. 182:2000;4628-4631.
14. Colland F., Fujita N., Ishihama A., Kolb A. The interaction between sigmaS, the stationary phase sigma factor, and the core enzyme of Escherichia coli RNA polymerase. Genes Cells. 7:2002;233-247.
15. Lee S.J., Gralla J.D. Open complex formation in vitro by sigma 38 (rpoS) RNA polymerase: roles for region 2 amino acids. J. Mol. Biol. 329:2003;941-948.
16. Studemann A., Noirclerc-Savoye M., Klauck E., Becker G., Schneider D., Hengge R. Sequential recognition of two distinct sites in sigma(S) by the proteolytic targeting factor RssB and ClpX. EMBO J. 22:2003;4111-4120.
17. Lange R., Hengge-Aronis R. The cellular concentration of the sigma S subunit of RNA polymerase in Escherichia coli is controlled at the levels of transcription, translation, and protein stability. Genes Dev. 8:1994;1600-1612.
18. Ivanova A., Renshaw M., Guntaka R.V., Eisenstark A. DNA base sequence variability in katF (putative sigma factor) gene of Escherichia coli. Nucleic Acids Res. 20:1992;5479-5480.
19. Atlung T., Nielsen H.V., Hansen F.G. Characterisation of the allelic variation in the rpoS gene in thirteen K12 and six other non-pathogenic Escherichia coli strains. Mol. Genet. Genom. 266:2002;873-881.
20. Visick J.E., Clarke S. RpoS- and OxyR-independent induction of HPI catalase at stationary phase in Escherichia coli and identification of rpoS mutations in common laboratory strains. J. Bacteriol. 179:1997;4158-4163.
21. Strom A.R., Kaasen I. Trehalose metabolism in Escherichia coli: stress protection and stress regulation of gene expression. Mol. Microbiol. 8:1993;205-210.
22. Almiron M., Link A.J., Furlong D., Kolter R. A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev. 6:1992;2646-2654.
23. Bolivar F., Rodriguez R.L., Greene P.J., Betlach M.C., Heyneker H.L., Boyer H.W. Construction and characterization of new cloning vehicles. II. A multipurpose cloning system. Gene. 2:1977;95-113.
24. Sambrook J., Russell D.W. Molecular Cloning: A Laboratory Manual. 2001;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
25. Aiba H., Adhya S., de Crombrugghe B. Evidence for two functional gal promoters in intact Escherichia coli cells. J. Biol. Chem. 256:1981;11905-11910.
26. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
27. Zambrano M.M., Siegele D.A., Almiron M., Tormo A., Kolter R. Microbial competition: Escherichia coli mutants that take over stationary phase cultures. Science. 259:1993;1757-1760.
28. Loewen P.C., Switala J., Triggs-Raine B.L. Catalases HPI and HPII in Escherichia coli are induced independently. Arch. Biochem. Biophys. 243:1985;144-149.
29. Chen H., Bjerknes M., Kumar R., Jay E. Determination of the optimal aligned spacing between the Shine-Dalgarno sequence and the translation initiation codon of Escherichia coli mRNAs. Nucleic Acids Res. 22:1994;4953-4957.
30. Barrick D., Villanueba K., Childs J., Kalil R., Schneider T.D., Lawrence C.E., Gold L., Stormo G.D. Quantitative analysis of ribosome binding sites in E. coli. Nucleic Acids Res. 22:1994;1287-1295.
31. Gold L. Posttranscriptional regulatory mechanisms in Escherichia coli. Annu. Rev. Biochem. 57:1988;199-233.
32. Shultzaberger R.K., Bucheimer R.E., Rudd K.E., Schneider T.D. Anatomy of Escherichia coli ribosome binding sites. J. Mol. Biol. 313:2001;215-228.
33. Rudd K.E. EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res. 28:2000;60-64.
34. Zambrano M.M., Kolter R. GASPing for life in stationary phase. Cell. 86:1996;181-184.
35. Finkel S.E., Kolter R. Evolution of microbial diversity during prolonged starvation. Proc. Natl. Acad. Sci. USA. 96:1999;4023-4027.
36. Sutton A., Buencamino R., Eisenstark A. rpoS mutants in archival cultures of Salmonella enterica serovar typhimurium. J. Bacteriol. 182:2000;4375-4379.
37. Cornelis S., Bruynooghe Y., Denecker G., Van Huffel S., Tinton S., Beyaert R. Identification and characterization of a novel cell cycle-regulated internal ribosome entry site. Mol. Cell. 5:2000;597-605.
38. Sanatinia H., Kofoid E.C., Morrison T.B., Parkinson J.S. The smaller of two overlapping cheA gene products is not essential for chemotaxis in Escherichia coli. J. Bacteriol. 177:1995;2713-2720.
39. Ozin A.J., Costa T., Henriques A.O., Moran C.P. Jr. Alternative translation initiation produces a short form of a spore coat protein in Bacillus subtilis. J. Bacteriol. 183:2001;2032-2040.