PMID:341159
| Citation |
Tamaki, S, Nakajima, S and Matsuhashi, M (1977) Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro. Proc. Natl. Acad. Sci. U.S.A. 74:5472-6 |
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| Abstract |
A thermosensitive mutant of Escherichia coli K-12 was isolated in which the membrane fractions were deficient both in penicillin-binding protein-1Bs, the major components of protein 1 [Spratt, B.G. & Pardee, A.B. (1975) Nature 254, 516-517] and in activity for in vitro peptidoglycan synthesis. The mutant was also supersensitive to many kinds of beta-lactam antibiotics. All these phenotypic changes were found to be caused by a single mutation (mrc). Genetic mapping studies show that the mrc mutation was located at about 3.3 min on the E. coli chromosome linkage map [Bachmann, B.J., Low, K.B. & Taylor, A.L. (1976) Bacteriol. Rev. 40, 116-167]. Penicillin-binding protein-1Bs seemed to be identical to one of the essential enzymes involved in crosslinking of peptidoglycan and the target of cell-lytic action of penicillins. Possible functions of some other penicillin-binding proteins in compensating for lack of protein-1Bs were also proposed. |
| Links | |
| Keywords |
Bacterial Proteins/genetics; Carrier Proteins/genetics; Chromosome Mapping; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli/metabolism; Hot Temperature; Mutation; Penicillins/metabolism; Penicillins/pharmacology; Peptidoglycan/biosynthesis |
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