High expression of the second lysine decarboxylase gene, ldc, in escherichia coli WC196 due to the recognition of the stop codon (TAG), at a position which corresponds to the 33th amino acid residue of σ38, as a serine residue by the amber suppressor, supD

Bioscience, Biotechnology and Biochemistry

Volumn 64, Issue 9, 2000, Pages 2012-2017

  Nagano, Takahiro ^a   Kikuchi, Yoshimi ^b   Kamio, Yoshiyuki ^a  

^a TOHOKU UNIVERSITY   (Japan)

^b AJINOMOTO CO INC   (Japan)

Author keywords

Amber suppressor supD; Escherichia coli W3110 38; Rpos; Rpos gene product ; Second lysine decarboxylase Ldc

Indexed keywords

AMINOACYL TRANSFER RNA; BACTERIAL PROTEIN; CARBOXYLYASE; LYSINE DECARBOXYLASE; RECOMBINANT PROTEIN; SIGMA FACTOR; SIGMA FACTOR KATF PROTEIN, BACTERIA; TRNA, SERINE; TRNA, SERINE-;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; DRUG EFFECT; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENETICS; KINETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; MUTAGENESIS; NUCLEOTIDE SEQUENCE; PLASMID; STOP CODON; SUPPRESSOR GENE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; CARBOXY-LYASES; CLONING, MOLECULAR; CODON, TERMINATOR; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENES, SUPPRESSOR; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PLASMIDS; RECOMBINANT PROTEINS; RNA, TRANSFER, AMINO ACYL; SIGMA FACTOR;

EID: 0034278180     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.64.2012     Document Type: Article

References (20)

1. Kikuchi, Y., Kojima, H., Tanaka, T., Takatsuka, Y., and Kamio, Y., Characterization of the second lysine decarboxylase isolated from Escherichia coli. J. Bac-teriol., 179, 4486-4492 (1997).
2. 38, is a second principal sigma factor of RNA polymerase in stationary phase Escherichia coli. Proc. Natl. Acad. Sei. U.S.A., 90, 3511-3515 (1993).
3. Kikuchi, Y., Kurahashi, O., Nagano, T., and Kamio, Y., RpoS-dependent expression of the second lysine decarboxylase gene in Escherichia coli. Biosci. Biotechnol. Biochem., 62, 1267-1270 (1998).
4. Mulvery, M. R., Switala, J., Borys, A., and Loewen, P. C., Regulation of transcription of katE and katF in Escherichia coli. J. Bacteriol., 172, 6173-6720 (1990).
5. Maurizi, M. R., Clark, W. P., Katayama, Y., Rudikoff, S., Pumphrey, J., Bowers, B., and Gottesman, S., Sequence and structure of ClpP, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem., 265, 12536-12545 (1990).
6. can be expressed independently from clpP in Escherichia coli. Biochem. Biophys. Res. Commun., 203, 798-804 (1994).
7. Zhou, Y. and Gottesman, S., Regulation of proteolysis of the stationary-phase sigma factor RpoS. J. Bac-teriol, 180, 1154-1158 (1998).
8. Olsen, A., Arnqvist, A., Hammar, M., Sukupolvi, S., and Normark, S., The RpoS sigma factor relieves H-NS-mediated transcriptional repression of csgA, the subunit gene of fibronectin-binding curli in Escherichia coli. Mol. Microbiol., 7, 523-536 (1993).
9. s subunit of RNA polymerase in Escherichia coli. J. Bacteriol., 179, 297-300 (1997).
10. gene of Escherichia coli. Nucleic Acids Res., 20, 5479-5480 (1992).
11. Strom, A. R. and Kaasen, I., Trehalose metabolism in Escherichia coli: stress protection and stress regulation of gene expression. Mol. Microbiol., 8, 205-210 (1993).
12. Styrvold, O. B. and Strom, A. R., Synthesis, accumulation and excretion of trehalose in osmotically stressed Escherichia coli K-12 strains: influence of amber suppressors and function of the periplasmic trehalase. J. Bacteriol., 173, 1188-1192 (1991).
13. Tate, W. P. and Mannering, S. A., Three, four or more: the translational stop signal at length. Mol. Microbiol., 21, 213-219 (1996).
14. Schagger, H. and von Jagow, G., Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368-379 (1987).
15. Van Dyke, M. W., Sirito, M., and Sawadogo, M., Single-step purification of bacterially expressed polypeptides containing an oligo-histidine domain. Gene, 111, 99-104 (1992).
16. Horton, R. M., Hunt, H. D., Ho, S. N., Pullen, J. K., and Pease, L. R., Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene, 77, 61-68 (1989).
17. Bachmann, B. J., Linkage map of Escherichia coli K-12, edition 8. Microbiol. Rev., 54, 130-197 (1990).
18. Amann, E., Ochs, B., and Abel, K. J., Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene, 69, 301-315 (1998).
19. Vieira, J. and Messing, J., The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene, 19, 259-268 (1982).
20. Bernardi, A. and Bernardi, F., Complete sequence of pSClOl. Nucleic Acids Res., 12, 9415-9426 (1984).