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Novel intermediates in the synthesis of maltose-binding protein in Escherichia coli

L L Randall, L G Josefsson, S J Hardy

    European Journal of Biochemistry
    |June 1, 1980
    PubMed

    Insights

    Nascent intermediates of maltose-binding protein were observed in Escherichia coli. Reduced mRNA elongation rates cause incomplete polypeptide accumulation, potentially aiding protein export.

    Area of Science:

    • Molecular Biology
    • Protein Synthesis
    • Cellular Biology

    Background:

    • Maltose-binding protein (MBP) is a periplasmic protein in Escherichia coli.
    • Protein translocation across the cytoplasmic membrane is essential for cellular function.

    Purpose of the Study:

    • To investigate nascent intermediates during maltose-binding protein synthesis.
    • To understand the role of mRNA elongation rates in protein synthesis and export.

    Main Methods:

    • In vivo and in vitro experiments were conducted.
    • Analysis of polypeptide intermediates and mRNA elongation rates.

    Main Results:

    • Nascent intermediates of maltose-binding protein were detected.
    • Evidence suggests a drastic reduction in mRNA elongation rates at specific sites.
    • Distinct species of incomplete polypeptides accumulated.

    Conclusions:

    • Reduced mRNA elongation rates lead to the accumulation of nascent intermediates.
    • These variations in elongation may play a role in the export of maltose-binding protein across the cytoplasmic membrane.

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