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Related Experiment Videos

Intrasubunit nucleotide binding in ribonucleic acid polymerase.

A D Malcolm, J R Moffatt

    The Biochemical Journal
    |October 1, 1978
    PubMed
    Summary
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    Periodate oxidation created modified nucleoside triphosphates that inhibit RNA polymerase. These modified nucleotides bind to a lysine residue in the enzyme

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Nucleoside triphosphates are essential substrates for RNA synthesis.
    • RNA polymerase is the enzyme responsible for transcription.
    • Understanding the active site of RNA polymerase is crucial for drug development.

    Purpose of the Study:

    • To synthesize novel derivatives of nucleoside triphosphates.
    • To investigate the inhibitory effects of these derivatives on RNA polymerase.
    • To identify the specific binding site of these inhibitors on RNA polymerase.

    Main Methods:

    • Periodate oxidation of the ribose ring in nucleoside triphosphates.
    • Incubation of oxidized nucleotides with Escherichia coli RNA polymerase and sodium borohydride (NaBH4).

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  • Analysis of labelled enzyme to identify the modified amino acid residue.

    • Main Results:

    • Synthesized oxidized nucleoside triphosphates act as competitive inhibitors of RNA polymerase.
    • Oxidized, labelled nucleotides form covalent bonds with Escherichia coli RNA polymerase.
    • A specific lysine residue within the alpha-subunit of RNA polymerase is identified as the labelled site.

    Conclusions:

    • The synthesized oxidized nucleoside triphosphates are potent inhibitors of RNA polymerase.
    • The covalent labeling identifies a lysine residue in the alpha-subunit as part of the nucleotide-binding site.
    • These findings provide insights into the structural organization of the RNA polymerase active site.