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Published January 25, 1983 | Published
Journal Article Open

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


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 (∽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.

Additional Information

© IRL Press Limited 1983. Received 29 September 1982; Revised 9 December 1982; Accepted 23 December 1982. We are greatly indebted to Louis Levinger, as well as James Barsoum and Daniel Finley for the many helpful discussions and advice. This work was supported by grants to A.V. from the National Cancer Institute and the National Institute of General Medical Sciences. P.S. was supported by a postdoctoral fellowship from Damon Runyon-Walter Winchel Cancer Fund, and earlier by a training grant (5T32-HL07146) from the National Institutes of Health.

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