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Clathrin-associated proteins contain bound nucleotide.

W J Schook, A Andrés, S Puszkin

    FEBS Letters
    |December 12, 1983
    PubMed
    Summary
    This summary is machine-generated.

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    Clathrin-associated proteins contain bound AMP/ADP, with phosphorylation varying by storage. This nucleotide binding may influence protein function.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Background:

    • Clathrin-associated proteins are crucial for cellular processes.
    • These proteins are known to interact with nucleotides.

    Purpose of the Study:

    • To investigate the nature of nucleotide binding in clathrin-associated proteins.
    • To understand the potential role of bound nucleotides in protein function.

    Main Methods:

    • Purification of clathrin-associated proteins from bovine brain.
    • Ultraviolet spectroscopy to determine absorbance maxima.
    • Thin-layer and high-performance liquid chromatography for nucleotide identification.
    • Analysis of nucleotide phosphorylation state under varying storage conditions.

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    Main Results:

    • Purified proteins showed an absorbance maximum at 256 nm.
    • Bound nucleotide was identified as adenosine monophosphate (AMP) and/or adenosine diphosphate (ADP).
    • The phosphorylation state of the bound nucleotide changed with storage.
    • A consistent molar ratio of two nucleotides per protein molecule was observed.
    • Evidence suggests potential exchange with adenosine triphosphate (ATP).

    Conclusions:

    • Clathrin-associated proteins tightly bind AMP/ADP.
    • The binding site and its nucleotide phosphorylation state may be functionally significant.
    • Further research is warranted to elucidate the precise role of nucleotide binding in clathrin-associated protein function.