Advances in Microbial Physiology, Volume 19 by A.H. Rose (Editor), J. Gareth Morris (Editor)

By A.H. Rose (Editor), J. Gareth Morris (Editor)

This quantity in a research-level sequence covers diversified points of microbial body structure and biochemistry together with inositol metabolisms in yeasts, bacterial adhesion, natural acids, the bacterial flagellum and the mechanical behaviour of bacterial mobilephone partitions. it's meant to be of use to microbiologists, biochemists and biotechnologists. different similar works during this sequence are volumes 29, 30 and 31.

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J. Rogers, unpublished work). Analysis of the effects of penicillin-binding proteins (Spratt and Pardee, 1975; Spratt, 1975) may be able to rationalize this somewhat chaotic situation. By using radioactively-labelled benzylpenicillin and competition experiments with other penicillins and cephalosporins for the six penicillin-binding proteins present in the cytoplasmic membranes of E. coli, three were selected as being connected with maintaining the normal morphology of cells. One, designated protein 3, was thought to control septation and was inactivated by combination with b-lactams.

This conclusion has been strengthened by isolation of two temperaturesensitive filamentous mutants of E. coli which both had a temperature- TABLE 2. Properties of the penicillin-binding proteins in the cytoplasmic membrane of Escherichia coli. -lactam low concentrations intermediate concentrations Lysis Ovoid cells Ovoid cells Filaments Filaments. Lysis Lysis Ovoid cells Lysis Filaments with bulges; lysis at higher concentrations Y 38 HOWARD J. ROGERS sensitive penicillin-binding protein 3 (Spratt, 1977a).

The pgmmutants also have very low autolytic activities and grow in normal media as chains of unseparated rods but, under phosphate limitation in chemostat cultures, the groups of round forms do not seem to be so large as those of the rod A mutant, possibly because the chains are TABLE 4.

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