Location of N-acetylmuramyl-L-alanyl-D-glutamylmesodiaminopimelic acid, presumed signal molecule for β-lactamase induction, in the bacterial cell

Antimicrobial Agents and Chemotherapy

Volumn 40, Issue 9, 1996, Pages 2173-2177

  Dietz, Helgard ^a   Pfeifle, Dieter ^a   Wiedemann, Bernd ^a  

^a UNIVERSITY OF BONN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BETA LACTAMASE; DIAMINOPIMELIC ACID; N ACETYLMURAMYLALANYL DEXTRO ISOGLUTAMINE DERIVATIVE; PEPTIDOGLYCAN; TRIPEPTIDE;

ARTICLE; BACTERIAL GENE; BACTERIAL METABOLISM; CONTROLLED STUDY; CYTOPLASM; ENTEROBACTER CLOACAE; ENZYME INDUCTION; ESCHERICHIA COLI K 12; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SIGNAL TRANSDUCTION;

EID: 0029796071     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.40.9.2173     Document Type: Article

References (26)

1. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
2. Broome-Smith, J., and B. G. Spratt. 1986. A vector for the construction of translational fusions to TEM beta-lactamase and the analysis of protein export signals and membrane protein topology. Gene 49:341-349.
3. Fleming, T. J., D. E. Wallsmith, and R. S. Rosenthal. 1986. Arthropathic properties of gonococcal peptidoglycan fragments: implications for the pathogenesis of disseminated gonococcal disease. Infect. Immun. 52:600-608.
4. Glauner, B., J.-V. Höltje, and U. Schwarz. 1988. The composition of the murein of Escherichia coli. J. Biol. Chem. 263:10088-10095.
5. Goodell, E. W. 1985. Recycling of murein by Escherichia coli. J. Bacteriol. 163:305-310.
6. Guest, J. R., and P. E. Stephens. 1980. Molecular cloning of the pyruvate dehydrogenase complex genes of Escherichia coli. J. Gen. Microbiol. 121: 277-292.
7. Heppel, L. A., and H. G. Nossal. 1966. The release of enzymes by osmotic shock from Escherichia coli in exponential phase. J. Biol. Chem. 241:3055-3062.
8. Höltje, J.-V., U. Kopp, A. Ursinus, and B. Wiedemann. 1994. The negative regulator of β-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase. FEMS Microbiol. Lett. 122:159-164.
9. Jacobs, C., L. Huang, E. Bartowsky, S. Normark, and J. T. Park. 1994. Bacterial cell wall recycling provides cytosolic muropeptides as effector for β-lactamase induction. EMBO J. 13:4684-4694.
10. Jacobs, C., B. Joris, M. Jamin, K. Klarsov, J. Van Beeumen, D. Mengin-Lecreulx, J. van Heijenoort, J. T. Park, and S. Normark. 1995. AmpD, essential for both β-lactamase regulation and cell wall recycling, is a novel cytosolic N-acetylmuramyl-L-alanine amidase. Mol. Microbiol. 15:553-559.
11. Kopp, U., B. Wiedemann, S. Lindquist, and S. Normark. 1993. Sequences of wild-type and mutant ampD genes of Citrobacter freundii and Enterobacter cloacae. Antimicrob. Agents Chemother. 37:224-228.
12. Korfmann, G., and C. C. Sanders. 1989. ampG is essential for high-level expression of AmpC β-lactamase in Enterobacter cloacae. Antimicrob. Agents Chemother. 33:1946-1951.
13. Korfmann, G., and B. Wiedemann. 1988. Genetic control of β-lactamase production in Enterobacter cloacae. Rev. Infect. Dis. 10:793-799.
14. Krueger, J. M., J. R. Pappenheimer, and M. L. Karnovsky. 1982. Sleep-promoting effects of muramylpeptides. Proc. Natl. Acad. Sci. USA 79:6102-6109.
15. Lindberg, F., S. Lindquist, and S. Normark. 1987. Inactivation of the ampD gene causes semiconstitutive overproduction of the inducible Citrobacter freundii β-lactamase. J. Bacteriol. 169:1923-1928.
16. Lindberg, F., and S. Normark. 1987. Common mechanism of ampC β-lactamase induction in enterobacteria: regulation of the cloned Enterobacter cloacae P99 β-lactamase gene. J. Bacteriol. 169:758-763.
17. Lindquist, S., M. Galleni, F. Lindberg, and S. Normark. 1989. Signaling proteins in enterobacterial AmpC β-lactamase regulation. Mol. Microbiol. 3:1091-1102.
18. Lindquist, S., F. Lindberg, and S. Normark. 1989. Binding of the Citrobacter freundii ampR regulator to a single DNA site provides both autoregulation and activation of the inducible ampC β-lactamase gene. J. Bacteriol. 171: 3746-3753.
19. Lindquist, S., K. Weston-Hafer, H. Schmidt, C. Pul, G. Korfmann, J. Erikson, C. Sanders, H. H. Martin, and S. Normark. 1993. AmpG, a signal transducer in chromosomal β-lactamase induction. Mol. Microbiol. 9:703-715.
20. Lodge, J. M., and L. J. V. Piddock. 1991. The control of class β-lactamase expression in Enterobacteriaceae and Pseudumonas aeruginosa. J. Antimicrob. Chemother. 28:167-172.
21. Normark, S., E. Bartowsky, J. Erickson, C. Jacobs, and F. Lindberg. 1994. Mechanism of chromosomal β-lactamase induction in gram-negative bacteria, p. 485-504. In J.-M. Ghuysen and R. Hakenberg (ed.), Bacterial cell wall. Elsevier, Amsterdam.
22. O'Callaghan, C. H., P. W. Muggleton, and G. W. Ross. 1969. Effects of β-lactamase from gram-negative organisms on cephalosporins and penicillins, p. 57-63. Antimicrob. Agents. Chemother. 1968.
23. Peter, K., G. Korfmann, and B. Wiedemann. 1988. Impact of AmpD gene and its production in Enterobacter cloacae. Rev. Infect. Dis. 10:800-805.
24. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
25. Tuomanen, E., B. Hengstler, O. Zak, and A. Tomasz. 1986. Induction of meningeal inflammation by diverse bacterial cell walls. Eur. J. Clin. Microbiol. 5:682-684.
26. Tuomanen, E., S. Lindquist, S. Sande, M. Galleni, K. Light, D. Gage, and S. Normark. 1991. Coordinate regulation of β-lactamase induction and peptidoglycan composition by the amp regulon. Science 251:201-204.