Previous Article | Next Article 
Antimicrob Agents Chemother. 1993 February; 37(2): 224-228
Sequences of wild-type and mutant ampD genes of Citrobacter freundii and Enterobacter cloacae.
U Kopp,
B Wiedemann,
S Lindquist and
S Normark
Institut für Medizinische Mikrobiologie und Immunologie, University of Bonn, Germany.
ABSTRACT
The ampD gene product regulates the expression of AmpC beta-lactamase in gram-negative bacteria and is proposed to be involved in peptidoglycan metabolism. In this study, we sequenced the ampD wild type and three mutant genes of Enterobacter cloacae and Citrobacter freundii. They exhibited a high degree of homology with the corresponding gene of Escherichia coli except in the carboxy termini, where, in the wild-type genes of E. cloacae and C. freundii, four additional amino acids yielding the Ser-X-X-Lys motif were found. Evidence that this C-terminal region of the ampD gene product is necessary for activity was shown by constructing a deletion of the last 16 amino acids. The spontaneous mutation of ampD02 is an out-of-frame insertion and yields an inactive AmpD protein. The single-base-pair substitution of Gly for Asp-121 in ampD05 is responsible for a hyperinducible phenotype. These results demonstrate regions of the ampD gene and the corresponding protein which have functional importance for the induction of AmpC beta-lactamase in E. cloacae.
Antimicrob Agents Chemother. 1993 February; 37(2): 224-228
This article has been cited by other articles:
-
Schmidtke, A. J., Hanson, N. D.
(2006). Model System To Evaluate the Effect of ampD Mutations on AmpC-Mediated {beta}-Lactam Resistance.. Antimicrob. Agents Chemother.
50: 2030-2037
[Abstract]
[Full Text]
-
Kaneko, K., Okamoto, R., Nakano, R., Kawakami, S., Inoue, M.
(2005). Gene Mutations Responsible for Overexpression of AmpC {beta}-Lactamase in Some Clinical Isolates of Enterobacter cloacae. J. Clin. Microbiol.
43: 2955-2958
[Abstract]
[Full Text]
-
Bagge, N., Ciofu, O., Hentzer, M., Campbell, J. I. A., Givskov, M., Hoiby, N.
(2002). Constitutive High Expression of Chromosomal {beta}-Lactamase in Pseudomonas aeruginosa Caused by a New Insertion Sequence (IS1669) Located in ampD. Antimicrob. Agents Chemother.
46: 3406-3411
[Abstract]
[Full Text]
-
Petrosino, J. F., Pendleton, A. R., Weiner, J. H., Rosenberg, S. M.
(2002). Chromosomal System for Studying AmpC-Mediated {beta}-Lactam Resistance Mutation in Escherichia coli. Antimicrob. Agents Chemother.
46: 1535-1539
[Abstract]
[Full Text]
-
Naas, T., Massuard, S., Garnier, F., Nordmann, P.
(2001). AmpD Is Required for Regulation of Expression of NmcA, a Carbapenem-Hydrolyzing {beta}-Lactamase of Enterobacter cloacae. Antimicrob. Agents Chemother.
45: 2908-2915
[Abstract]
[Full Text]
-
Mimoz, O., Leotard, S., Jacolot, A., Padoin, C., Louchahi, K., Petitjean, O., Nordmann, P.
(2000). Efficacies of Imipenem, Meropenem, Cefepime, and Ceftazidime in Rats with Experimental Pneumonia Due to a Carbapenem-Hydrolyzing beta -Lactamase-Producing Strain of Enterobacter cloacae. Antimicrob. Agents Chemother.
44: 885-890
[Abstract]
[Full Text]
-
Kuga, A., Okamoto, R., Inoue, M.
(2000). ampR Gene Mutations That Greatly Increase Class C beta -Lactamase Activity in Enterobacter cloacae. Antimicrob. Agents Chemother.
44: 561-567
[Abstract]
[Full Text]
-
Langaee, T. Y., Gagnon, L., Huletsky, A.
(2000). Inactivation of the ampD Gene in Pseudomonas aeruginosa Leads to Moderate-Basal-Level and Hyperinducible AmpC beta -Lactamase Expression. Antimicrob. Agents Chemother.
44: 583-589
[Abstract]
[Full Text]
-
Langaee, T. Y., Dargis, M., Huletsky, A.
(1998). An ampD Gene in Pseudomonas aeruginosa Encodes a Negative Regulator of AmpC beta -Lactamase Expression. Antimicrob. Agents Chemother.
42: 3296-3300
[Abstract]
[Full Text]
-
Votsch, W., Templin, M. F.
(2000). Characterization of a beta -N-acetylglucosaminidase of Escherichia coli and Elucidation of Its Role in Muropeptide Recycling and beta -Lactamase Induction. J. Biol. Chem.
275: 39032-39038
[Abstract]
[Full Text]
Copyright © 1993 by the American Society for Microbiology. All rights reserved.