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J. Biol. Chem., Vol. 279, Issue 5, 3382-3388, January 30, 2004

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Histone Tail-independent Chromatin Binding Activity of Recombinant Cohesin Holocomplex^*

Alexander Kagansky, Lita Freeman, Dmitry Lukyanov, and Alexander Strunnikov

From the Laboratory of Gene Regulation and Development, NICHD, National Institutes of Health, Bethesda, Maryland 20892

Cohesin, an SMC (structural maintenance of chromosomes) protein-containing complex, governs several important aspects of chromatin dynamics, including the essential chromosomal process of sister chromatid cohesion. The exact mechanism by which cohesin achieves the bridging of sister chromatids is not known. To elucidate this mechanism, we reconstituted a recombinant cohesin complex and investigated its binding to DNA fragments corresponding to natural chromosomal sites with high and low cohesin occupancy in vivo. Cohesin displayed uniform but nonspecific binding activity with all DNA fragments tested. Interestingly, DNA fragments with high occupancy by cohesin in vivo showed strong nucleosome positioning in vitro. We therefore utilized a defined model chromatin fragment (purified reconstituted dinucleosome) as a substrate to analyze cohesin interaction with chromatin. The four-subunit cohesin holocomplex showed a distinct chromatin binding activity in vitro, whereas the Smc1p-Smc3p dimer was unable to bind chromatin. Histone tails and ATP are dispensable for cohesin binding to chromatin in this reaction. A model for cohesin association with chromatin is proposed.

Received for publication, June 10, 2003 , and in revised form, October 28, 2003.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains a Western blot demonstrating the sensitivity of the cohesion complex to ATP depletion.

Supported by the National Institutes of Health Graduate Partnership Program.

To whom correspondence should be addressed: LGRD, NICHD, National Institutes of Health, 18T Library Dr., Rm. 106, Bethesda, MD 20892. Tel.: 301-402-8384; Fax: 301-402-1323; E-mail: strunnik{at}box-s.nih.gov.

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