Abstract
Properties of the Caulobacter penicillin-binding proteins (PBPs) were studied. Several Caulobacter strains possessed at least five major PBPs, as shown previously for C. crescentus CB15, namely PBP1A, PBP1Bs, PBP2, PBP3 and PBP4. PBP4 was not detected in the C. crescentus strain CB13. None of the strains examined possessed the major PBPs of low molecular weight which have been found in other species of bacteria. The biochemical properties of the Caulobacter PBPs were studied further with two strains, C. crescentus CB13 and C. crescentus CB15. In these strains, PBPs of similar molecular weight were similar in properties such as affinity for β-lactam antibiotics and heat sensitivity. These properties were markedly different from those of PBPs of Escherichia coli and other bacteria. To elucidate the functions of the Caulobacter PBPs, the effects of several β-lactam antibiotics on cell morphology and their affinities for different PBPs were examined. The relationship between the antibiotic effect and its affinity for PBPs suggests that PBP3 is involved in the process of cell division.
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