Loss or overproduction of polypeptide release factor 3 influences expression of the tryptophanase operon of Escherichia coli

Journal of Bacteriology

Volumn 178, Issue 13, 1996, Pages 3755-3762

  Yanofsky, Charles ^a   Horn, Virginia ^a   Nakamura, Yoshikazu ^b  

^a STANFORD UNIVERSITY   (United States)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; BICOZAMYCIN; CYCLIC AMP; GLUCOSE; SIGNAL PEPTIDE; TRYPTOPHAN; TRYPTOPHANASE;

ANTIBIOTIC RESISTANCE; ARTICLE; BACTERIUM CULTURE; CULTURE MEDIUM; ENZYME ASSAY; ENZYME SYNTHESIS; ESCHERICHIA COLI; GENE ACTIVATION; GENE EXPRESSION; GENE MUTATION; NONHUMAN; OPERON; PRIORITY JOURNAL; PROTEIN EXPRESSION; STOP CODON;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; TRIXIS;

EID: 0030013069     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.13.3755-3762.1996     Document Type: Article

References (37)

1. Adamski, F. M., K. M. McCaughan, F. Jorgensen, C. G. Kurland, and W. P. Tate. 1994. The concentration of polypeptide chain release factors 1 and 2 at different growth rates of Escherichia coli. J. Mol. Biol. 238:302-308.
2. Botsford, J. L. 1975. Metabolism of cyclic 3′,5′-adenosine monophosphate and induction of tryptophanase in Escherichia coli. J. Bacteriol. 124:380-390.
3. Botsford, J. L., and R. D. DeMoss. 1971. Cataholite repression of tryptophanase in Escherichia coli. J. Bacteriol. 105:303-312.
4. Brown, C. M., and W. P. Tate. 1994. Direct recognition of mRNA stop signals by Escherichia coli polypeptide chain release factor two. J. Biol. Chem. 269:33164-33170.
5. Burns, C. M., and J. P. Richardson. 1995. NusG is required to overcome a kinetic limitation to Rho function at an intragenic terminator. Proc. Natl. Acad. Sci. USA 92:4738-4742.
6. Court, D. L., T. A. Patterson, T. Baker, N. Constatino, X. Mao, and D. I. Friedman. 1995. Structural and functional analyses of the transcription-translation proteins NusB and NusE. J. Bacteriol. 177:2589-2591.
7. Deeley, M. C., and C. Yanofsky. 1981. Nucleotide sequence of the structural gene for tryptophanase of Escherichia coli K-12. J. Bacteriol. 147:787-796.
8. Deeley, M. C., and C. Yanofsky. 1982. Transcription initiation at the tryptophanase promoter of Escherichia coli K-12. J. Bacteriol. 151:942-951.
9. Eshoo, M., and C. Yanofsky. Unpublished data.
10. Friedman, D. I. 1988. Regulation of phage gene expression by termination and antitermination of transcription, p. 263-319. In R. Calender (ed.). The bacteriophages, vol. 2. Plenum Publishing Co., New York.
11. Gish, K., and C. Yanofsky. 1993. Inhibition of expression of the tryptophanase operon in Escherichia coli by extrachromosomal copies of the tna leader region. J. Bacteriol. 175:3380-3387.
12. Gish, K., and C. Yanofsky. 1995. Evidence suggesting cis action by the TnaC leader peptide in regulating transcription attenuation in the tryptophanase operon of Escherichia coli. J. Bacteriol. 177:7245-7254.
13. Trp translation of leader peptide codon 12 and other factors that regulate expression of the tryptophanase operon. J. Bacteriol. 172:3100-3107.
14. Grentzmann, G., D. Brechemier-Baey, V. Heurgue, L. Mora. and R. H. Buckingham. 1994. Localization and characterization of the gene encoding release factor RF3 in Escherichia coli. Proc. Natl. Acad. Sci. USA 91:5848-5852.
15. Grentzmann, G., D. Brechemier-Baey, V. Heurgue-Hamard, and R. H. Buckingham. 1995. Function of polypeptide chain release factor RF3 in Escherichia coli. J. Biol. Chem. 270:10595-10600.
16. Isaacs, H., Jr., D. Chao, C. Yanofsky, and M. H. Saier, Jr. 1994. Mechanism of catabolite repression of tryptophanase synthesis in Escherichia coli. Microbiology (Reading) 140:2125-2134.
17. Ito, K., K. Ebihara, M. Uno, and Y. Nakamura. Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis. Proc. Natl. Acad. Sci. USA, in press.
18. Ito, K., and Y. Nakamura. Unpublished data.
19. Janosi, L., I. Shimizu, and A. Kaji. 1994. Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth. Proc. Natl. Acad. Sci. USA 91:44249-44253.
20. Kamath, A., and C. Yanofsky. 1992. Characterization of the tryptophan operon of Proteus vulgaris: cloning, nucleotide sequence, amino acid homology, in vitro synthesis of the leader peptide and regulatory analysis. J. Biol. Chem. 267:19978-19985.
21. Kawakami, K., T. Inada, and Y. Nakamura. 1988. Conditional lethal and recessive UGA-suppressor mutations in the prfB gene encoding peptide chain release factor 2 of Escherichia coli. J. Bacteriol. 170:5378-5381.
22. Kawazu, Y., K. Ito, K. Matsumura, and Y. Nakamura. 1995. Comparative characterization of release factor RF-3 genes of Escherichia coli, Salmonella typhimurium, and Dichelobacter nodosus. J. Bacteriol. 177:5547-5553.
23. Li, J., S. D. Mason, and J. Greenblatt. 1993. Elongation factor NusG interacts with the termination factor Rho to regulate termination and antitermination of transcription. Genes Dev. 7:161-172.
24. Matsumura, K., K. Ito, Y. Kawazu, O. Mikuni, and Y. Nakamura. 1996. Suppression of temperature-sensitive defects of polypeptide release factors RF-1 and RF-2 by mutations or by an excess of RF-3 in Escherichia coli. J. Mol. Biol. 258:588-599.
25. Mikuni, O., K. Ito, J. Moffat, K. Matsumura, K. McCaughan, T. Nobukuni, W. Tate, and Y. Nakamura. 1994. Identification of the prfC gene, which encodes peptide-chain-rclease factor 3 of Escherichia coli. Proc. Natl. Acad. Sci. USA 91:5798-5802.
26. Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
27. Sarsero, J. P., P. J. Wookey, P. Gollnick, C. Yanofsky, and A. J. Pittard. 1991. A new family of integral membrane proteins involved in the transport of aromatic amino acids in Escherichia coli. J. Bacteriol. 173:3231-3234.
28. Stewart, V. J., R. Landick, and C. Yanofsky. 1986. Rho-dependent transcription termination in the tryptophanase operon leader region of Escherichia coli K-12. J. Bacteriol. 166:217-233.
29. Stewart, V. J., and C. Yanofsky. 1985. Evidence for transcription antitermination control of tryptophanase gene expression in Escherichia coli K-12. J. Bacteriol. 164:731-740.
30. Stewart, V. J., and C. Yanofsky. 1986. Role of leader peptide synthesis in tryptophanase operon expression in Escherichia coli K-12. J. Bacteriol. 167:383-386.
31. Suelter, C. H., J. Wang, and E. E. Snell. 1976. Direct spectrophotometric assay of tryptophanase. FEES Lett. 66:230-232.
32. Sullivan, S., and M. E. Gottesman. 1992. Requirement for E. coli NusG protein in factor-dependent transcription termination. Cell 68:989-994.
33. Vogel, H., and D. Bonner. 1956. Acetylornithinase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218:97-106.
34. Vogel, U., and K. F. Jensen. 1995. Effects of the antiterminator BoxA on transcription elongation kinetics and ppGpp inhibition of transcription elongation in Escherichia coli. J. Biol. Chem. 270:18335-18340.
35. Yanofsky, C., and V. Horn. 1995. Bicyclomycin sensitivity and resistance affect Rho factor-mediated transcription termination in the tna operon of Escherichia coli. J. Bacteriol. 177:4451-4456.
36. Yanofsky, C., V. Horn, and P. Gollnick. 1991. Physiological studies on tryptophan transport and tryptophanase operon induction in Escherichia coli. J. Bacteriol. 173:6009-6017.
37. Zwiefka, A., H. Kohn, and W. R. Widger. 1993. Transcription termination factor rho: the site of bicyclomycin inhibition in Escherichia coli. Biochemistry 32:3564-3570.