DsbA-insensitive expression of CcrA, a metallo-β-lactamase from Bacteroides fragilis, in Escherichia coli after amino acid substitution at two cysteine residues within CcrA

Journal of Bacteriology

Volumn 178, Issue 14, 1996, Pages 4306-4309

  Alksne, Lefa E ^a   Rasmussen, Beth A ^a  

^a PFIZER INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE; CYSTEINE; BACTERIAL PROTEIN; CARBAPENEMASE; ISOMERASE; METALLOPROTEIN; PROTEIN DISULFIDE ISOMERASE; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BACTEROIDES FRAGILIS; CONTROLLED STUDY; CYTOPLASM; DISULFIDE BOND; ESCHERICHIA COLI; GENE EXPRESSION; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; ENZYMOLOGY; GENETICS; METABOLISM;

BACTERIAL PROTEINS; BACTEROIDES FRAGILIS; BETA-LACTAMASES; CYSTEINE; ESCHERICHIA COLI; ISOMERASES; METALLOPROTEINS; PROTEIN DISULFIDE-ISOMERASE; RECOMBINANT PROTEINS;

EID: 0029666063     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.14.4306-4309.1996     Document Type: Article

References (18)

1. Akiyama, Y., S. Kamitani, N. Kusukawa, and K. Ito. 1992. In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product. J. Biol. Chem. 267:22440-22445.
2. Alksne, L. E., R. A. Anthony, S. W. Liebman, and J. R. Warner. 1993. An accuracy center in the ribosome conserved over 2 billion years. Proc. Natl. Acad. Sci. USA 90:9538-9541.
3. Alksne, L. E., D. Keeney, and B. A. Rasmussen. 1995. A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-β-lactamase, CcrA, in Escherichia coli. J. Bacteriol. 177:462-464.
4. Bardwell, J. C. A. 1994. Building bridges: disulphide bond formation in the cell. Mol. Microbiol. 14:199-205.
5. Bardwell, J. C. A., J. Lee, G. Jander, N. Martin, D. Belin, and J. Beckwith. 1993. A pathway for disulfide bond formation in vivo. Proc. Natl. Acad. Sci. USA 90:1038-1042.
6. Casadaban, M. J., and S. N. Cohen. 1980. An analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138:459-463.
7. Higuchi, R., B. Krummel, and R. K. Saiki. 1988. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16:7351-7367.
8. Kamitani, S., Y. Akiyama, and K. Ito. 1992. Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. EMBO J. 11:57-62.
9. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 277:680-685.
10. Missiakas, D., C. Georgopoulos, and S. Raina. 1993. Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo. Proc. Natl. Acad. Sci. USA 90:7084-7088.
11. Missiakas, D., C. Georgopoulos, and S. Raina. 1994. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 13:2013-2020.
12. Osano, E., Y. Arakawa, R. Wacharotayankun, M. Ohta, T. Horii, H. Ito, F. Yoshimura, and N. Kato. 1994. Molecular characterization of an enterobacterial metallo-β-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance. Antimicrob. Agents Chemother. 38:71-78.
13. Rasmussen, B. A., Y. Gluzman, and F. P. Tally. 1990. Cloning and sequencing of the class B β-lactamase gene (ccrA) from Bacteroides fragilis TAL3636. Antimicrob. Agents Chemother. 34:1590-1592.
14. Rasmussen, B. A., Y. Gluzman, and F. P. Tally. 1991. Escherichia coli chromosomal mutations that permit direct cloning of the Bacteroides fragilis metallo-β-lactamase gene, ccrA. Mol. Microbiol. 5:1211-1219.
15. Rasmussen, B. A., Y. Yang, N. Jacobus, and K. Bush. 1994. Contribution of enzymatic properties, cell permeability, and enzyme expression to microbiological activities of β-lactams in three Bacteroides fragilis isolates that harbor a metallo-β-lactamase gene. Antimicrob. Agents Chemother. 38:2116-2120.
16. Shevchik, V. E., G. Condemine, and J. Robert-Baudouy. 1994. Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J. 13:2007-2012.
17. Wolfson, J. S., D. C. Hooper, M. N. Swartz, M. D. Swartz, and G. L. McHugh. 1983. Rapid method for screening large numbers of Eschenchia coli colonies for production of plasmid-mediated β-lactamases. Antimicrob. Agents Chemother. 23:308-312.
18. Zapun, A., D. Missiakas, S. Raina, and T. E. Creighton. 1995. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34:5075-5089.