JBC Focus on PI3-Kinase with Echelon

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Volume 271, Number 51, Issue of December 20, 1996 pp. 32580-32585
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

H1 Binding Unwinds DNA
EVIDENCE FROM TOPOLOGICAL ASSAYS

(Received for publication, June 12, 1996, and in revised form, October 7, 1996)

Maria Ivanchenko Dagger , Ahmed Hassan Dagger , Kensal van Holde Dagger and Jordanka Zlatanova Dagger §

From Dagger  Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331-7305 and § Institute of Genetics, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria

The preference of the linker histones to bind to superhelical DNA in comparison with linear or relaxed molecules suggests that these proteins might, in turn, change the twist and/or writhe of DNA molecules upon binding. In order to explore such a possibility, we looked for changes in the linking number of plasmid pBR322 caused by H1 binding, using assays that involve nicking and resealing of DNA strands. Two types of enzymes were used, eukaryotic topoisomerase I and prokaryotic DNA ligase. The results revealed that H1 binding causes unwinding of the DNA, with the unwinding angle being approximately 10°. The globular domain of histone H1 is also capable of unwinding DNA, but to a lesser degree.


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