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Sequence sensitivity of histone binding.

I M Leffak, H J Li

    Biochimica Et Biophysica Acta
    |November 27, 1981
    PubMed
    Summary
    This summary is machine-generated.

    Histones exhibit varying preferences for DNA sequences, with some showing a higher affinity for AT-rich regions. However, histone interactions within nucleosomes reduce this sequence selectivity.

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    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Genetics

    Background:

    • Histones are crucial proteins that package DNA into nucleosomes.
    • The interaction between histones and DNA sequence is fundamental to genome organization and regulation.
    • Understanding histone-DNA binding selectivity is key to deciphering epigenetic mechanisms.

    Purpose of the Study:

    • To investigate the nucleotide sequence selectivity of different histone fractions during DNA binding.
    • To determine how histone-histone interactions influence DNA sequence preference in nucleosome formation.

    Main Methods:

    • Reconstitution of nucleoproteins using purified histone fractions and DNA of varying base compositions.
    • Thermal denaturation assays to measure DNA-histone binding.

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  • In vitro reconstitution under varying salt and urea concentrations to mimic physiological conditions.

    • Main Results:

    • A distinct (A + T)-binding preference was observed for individual histone fractions, with H1 showing the highest preference.
    • The order of decreasing (A + T)-binding preference was H1 > H2B > H5 > H2A > [H2A + H2B] > [H2A + H2B + H3 + H4] > [H1 + (H2A + H2B + H3 + H4)2].
    • Nucleosome complexes formed under physiologically comparable conditions exhibited minimal (A + T)-binding preference, indicating reduced sequence selectivity.

    Conclusions:

    • Individual histone fractions display varying degrees of nucleotide sequence selectivity.
    • Homotypic and heterotypic histone interactions significantly decrease the sequence selectivity of DNA binding during nucleosome assembly.
    • These findings highlight the role of histone complex formation in modulating DNA-protein interactions within chromatin.