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Biosynthesis of a plasmid-encoded outer membrane surface exclusion protein involves processing from a precursor

D Ferrazza, S B Levy

    The Journal of Biological Chemistry
    |October 10, 1980
    PubMed
    Summary
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    Researchers identified a precursor to the R222 plasmid-encoded outer membrane protein MRB in Escherichia coli. This precursor is processed into mature MRB, similar to host cell membrane protein processing.

    Area of Science:

    • Molecular Biology
    • Microbiology
    • Protein Biochemistry

    Background:

    • MRB (Major R222 plasmid-encoded outer membrane protein) is an outer membrane protein encoded by the R222 plasmid.
    • MRB is immunologically identical to the traTp protein of the F plasmid.

    Purpose of the Study:

    • To investigate the processing of the MRB protein in Escherichia coli.
    • To determine if plasmid-encoded membrane proteins undergo processing similar to host cell proteins.

    Main Methods:

    • Detection of MRB precursor using specific anti-MRB serum in Escherichia coli minicells.
    • Use of proteolytic inhibitors to stabilize precursor polypeptides.
    • Pulse-chase experiments with [35S]methionine to track precursor conversion to mature MRB.
    • Inhibition studies using tosyllysylalanyl chloramethyl ketone.

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    Main Results:

    • An apparent precursor polypeptide of MRB was detected in Escherichia coli minicells.
    • The precursor was found in cells containing R222 or F plasmids, especially in the presence of proteolytic inhibitors.
    • Pulse-chase experiments demonstrated the conversion of the precursor to mature MRB.
    • This conversion was inhibited by tosyllysylalanyl chloramethyl ketone, indicating a proteolytic processing step.

    Conclusions:

    • Plasmid-encoded outer membrane proteins, such as MRB, are processed in Escherichia coli.
    • The processing mechanism for MRB resembles that of host cell membrane proteins.
    • This suggests a conserved pathway for membrane protein maturation in bacteria.