HMG 14/17 binding affinities and DNAase I sensitivities of nucleoprotein particles | Zendy

A. Stein | Zendy; T. Matthew Townsend | Zendy

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HMG 14/17 binding affinities and DNAase I sensitivities of nucleoprotein particles

Author(s) -

A. Stein,

T. Matthew Townsend

Publication year - 1983

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/11.19.6803

Subject(s) - nucleosome , biology , micrococcal nuclease , nucleoprotein , dna , chromatin , microbiology and biotechnology , nuclease , deoxyribonuclease i , biochemistry , deoxyribonuclease , nucleotide , biophysics , base sequence , gene

We show that ordinary (bulk) chicken erythrocyte nucleosomes are digested more rapidly by DNAase I when they are associated with high mobility group (HMG) proteins 14/17. Digestion of HMG 14/17-nucleosome complexes, under conditions where the DNA in control nucleosomes is digested to 10 to 20% acid solubility, results in a particular depletion of single-strand DNA fragments greater than 80 nucleotides in length, relative to the DNA fragments produced from control nucleosomes. Additionally, we show that staphylococcal nuclease digests of H1/H5-depleted chromatin contain an abundant subclass of nucleosomes that are not present in appreciable amounts in digests of native chromatin. These nucleosomes contain longer lengths of DNA and have lower electrophoretic mobilities than core particles. HMG 14/17 associates highly preferentially with these nucleosomes and renders them sensitive to DNAase I, similar to what has been found for active nucleosomes.

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