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Thiol proteins in chromatin.

A Ferraro, A Giartosio, M Eufemi

    Bioscience Reports
    |March 1, 1986
    PubMed
    Summary
    This summary is machine-generated.

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    Researchers measured half-cystine residues in pig liver chromatin proteins. These thiol (SH) and disulfide (SS) groups appear crucial for chromatin structure and function, particularly in non-histone proteins.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Chromatin Structure

    Background:

    • Chromatin structure is influenced by protein modifications.
    • The role of thiol and disulfide bonds in chromatin is not fully understood.

    Purpose of the Study:

    • To quantify half-cystine residues in pig liver chromatin.
    • To investigate the distribution and potential role of thiol (SH) and disulfide (SS) groups in chromatin.

    Main Methods:

    • Quantification of total half-cystine residues in pig liver chromatin proteins.
    • Analysis of thiol group distribution in relation to chromatin solubility using DNase I and DNase II.

    Main Results:

    • Approximately half of the total half-cystine residues in pig liver chromatin proteins are in the reduced state.

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  • Non-histone chromatin proteins contain about 40 nmol/mg of protein thiol groups.
  • These thiol groups are concentrated in chromatin fractions readily solubilized by DNases.

    • Conclusions:

    • The presence and distribution of SH and SS groups suggest their involvement in maintaining chromatin structure.
    • Thiol groups on non-histone proteins may play a role in chromatin organization and accessibility.