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Nucleic Acids Research, 1983, Vol. 11, No. 2 387-401
© 1983

MOLECULAR BIOLOGY

Affinity of HMG17 for a mononucleosome is not influenced by the presence of ubiquitin-H2A semihistone but strongly depends on DNA fragment size

Paul S. Swerdlow1,2 and Alexander Varshavsky1

1Department of Biology, Massachusetts Institute of Technology Cambridge, MA 02139 2Division of Hematology-Oncology, Department of Medicine, Children's Hospital Medical Center Boston, MA 02115, USA

Received September 29, 1982. Revised December 9, 1982. Accepted December 23, 1982.

We have used a two-dimensional (deoxyribonucleoprotein ->DNA) electrophoretic binding assay to study the interaction of the purified high mobility group protein HMG17 with isolated HeLa mononucleosomes as a function of their DNA fragment size and the presence of ubiquitin-H2A semihistone. No significant differences between affinities of HMG17 for ubiquitinated and non-ubiquitinated core mononucleosomes were observed. In striking contrast, the apparent affinity of HMG17 for a mononucleosome increases more than 100-fold upon an increase of the length of the mononucleosomal DNA fragment by as few as 3 to 5 bp over the core DNA length ({bsim}146 bp). We suggest that the magnitude of this effect is sufficient to explain the preferential binding of HMG17 in vitro to mononucleosomes derived from actively transcribed genes.


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