Protein Targeting to the Bacterial Cytoplasmic Membrane

Peter Fekkes, Arnold J.M. Driessen

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    Abstract

    Proteins that perform their activity within the cytoplasmic membrane or outside this cell boundary must be targeted to the translocation site prior to their insertion and/or translocation. In bacteria, several targeting routes are known; the SecB- and the signal recognition particle-dependent pathways are the best characterized. Recently, evidence for the existence of a third major route, the twin-Arg pathway, was gathered Proteins that use either one of these three different pathways possess special features that enable their specific interaction with the components of the targeting routes. Such targeting information is often contained in an N-terminal extension, the signal sequence, but can also be found within the mature domain of the targeted protein. Once the nascent chain starts to emerge from the ribosome, competition for the protein between different targeting factors begins. After recognition and binding, the targeting factor delivers the protein to the translocation sires at the cytoplasmic membrane. Only by means of a specific interaction between the targeting component and its receptor is the cargo released for further processing and translocation. This mechanism ensures the high-fidelity targeting of premembrane and membrane proteins to the translocation site.
    Original languageEnglish
    Pages (from-to)161 - 173
    Number of pages14
    JournalMicrobiology and Molecular Biology Reviews
    Volume63
    Issue number1
    Publication statusPublished - Mar-1999

    Keywords

    • SIGNAL-RECOGNITION PARTICLE
    • MALTOSE-BINDING-PROTEIN
    • ESCHERICHIA-COLI SECB
    • ENDOPLASMIC-RETICULUM MEMBRANE
    • MOLECULAR CHAPERONES GROEL
    • HEAT-SHOCK PROTEINS
    • MATURE LAMB PROTEIN
    • DELTA-MU-H+
    • PRECURSOR PROTEIN
    • INNER-MEMBRANE

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