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Penicillin-binding proteins in Bacillus subtilis mutants.

G Kleppe, W Yu, J L Strominger

    Antimicrobial Agents and Chemotherapy
    |June 1, 1982
    PubMed
    Summary

    Penicillin-binding proteins (PBPs) in Bacillus subtilis mutants were analyzed. Alterations in specific PBPs correlated with morphological changes, including size reduction and helical formation, offering insights into bacterial cell wall synthesis.

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    Molecular and cellular biology·1992

    Area of Science:

    • Microbiology
    • Molecular Biology
    • Biochemistry

    Background:

    • Penicillin-binding proteins (PBPs) are essential enzymes involved in bacterial cell wall synthesis and are targets for antibiotics.
    • Understanding the relationship between PBP structure, function, and cell morphology is crucial for deciphering bacterial growth and division mechanisms.

    Purpose of the Study:

    • To investigate the alterations in penicillin-binding proteins (PBPs) in various Bacillus subtilis mutants.
    • To correlate observed changes in PBPs with specific morphological phenotypes.

    Main Methods:

    • Analysis of penicillin-binding proteins (PBPs) in Bacillus subtilis mutants using sodium dodecyl sulfate gel electrophoresis.
    • Comparison of PBP profiles and quantities between mutant strains and the wild-type parent strain.
    • Morphological characterization of the studied Bacillus subtilis mutants.

    Main Results:

    • A cloxacillin-resistant mutant exhibited altered and increased amounts of PBP 2a, with a concomitant absence of PBPs 1a and 1b, leading to a 15% decrease in cell size.
    • Two morphological mutants (Tr49, small diameter; Tr61, helical form) showed no changes in the total number of PBPs compared to the parent strain.
    • Mutant Tr49 displayed altered mobility for PBPs 1a and 1b.

    Conclusions:

    • Specific alterations in penicillin-binding proteins (PBPs), such as PBP 2a, PBP 1a, and PBP 1b, are associated with distinct morphological changes in Bacillus subtilis.
    • These findings contribute to understanding the complex roles of individual PBPs in bacterial cell wall construction and shape determination.

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