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Nucleic Acids Research, 1983, Vol. 11, No. 19 6803-6819
© 1983

MOLECULAR BIOLOGY

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

A. Stein* and T. Townsend

Department of Biological Sciences, Purdue University W. Lafayette, IN 47907, USA

*To whom correspondence should be addressed

Received May 15, 1983. Revised September 12, 1983. Accepted September 12, 1983.

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-nucleoaome 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 then 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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H. Ding, S Rimsky, S. Batson, M Bustin, and U Hansen
Stimulation of RNA polymerase II elongation by chromosomal protein HMG-14
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[Abstract] [PDF]


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