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[ATP-dependent structural changes in chromatin]

V I Tiulenev, L A Konoplich, A A Krivonos

    Biokhimiia (Moscow, Russia)
    |August 1, 1993
    PubMed
    Summary
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    [Effect of adenosine triphosphate on the cleavage of H1 histones in nuclei of rat spleen and liver].

    Ukrainskii biokhimicheskii zhurnal (1978)·1996

    Adenosine triphosphate (ATP) prevents histone proteolysis in guinea pig spleen chromatin. ATP protects nuclear proteins from degradation while promoting cleavage of cytosolic proteins, suggesting a role in chromatin structural regulation.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Context:

    • Nuclear and chromatin proteins are susceptible to proteolysis.
    • Specific histone proteolysis (H1 and H2A) occurs in guinea pig spleen nuclei and chromatin.
    • This proteolysis results in the accumulation of specific hydrolytic products.

    Purpose:

    • To investigate the effect of adenosine triphosphate (ATP) on histone proteolysis in guinea pig spleen nuclei and chromatin.
    • To identify the protective role of ATP against proteinase activity.
    • To explore ATP-dependent mechanisms of chromatin structural rearrangement.

    Summary:

    • Incubation of guinea pig spleen nuclei and chromatin led to proteolysis of H1 and H2A histones.
    • Sodium dodecyl sulfate gel electrophoresis confirmed the decline of H1 and H2A and the appearance of new protein bands.

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  • Adenosine triphosphate (ATP) addition inhibited H1 and H2A digestion and the formation of hydrolytic products.
  • ATP also promoted the cleavage of low molecular weight cytosolic proteins.

    • Impact:

    • ATP acts as a protective agent for nuclear and chromatin proteins against proteolysis.
    • ATP influences chromatin structure, rendering nuclear proteins resistant to degradation.
    • The findings suggest a regulatory role for ATP in maintaining chromatin integrity and potentially controlling gene expression.