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Originally published In Press as doi:10.1074/jbc.M011153200 on February 2, 2001

J. Biol. Chem., Vol. 276, Issue 18, 14597-14601, May 4, 2001
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Magnesium-dependent Association and Folding of Oligonucleosomes Reconstituted with Ubiquitinated H2A*

Laure J. M. JasonDagger §, Susan C. Moore, Juan Ausió, and George LindseyDagger

From the Dagger  Department of Biochemistry, University of Cape Town, Private Bag, Rondebosch 7701, South Africa and the  Department of Biochemistry and Microbiology, University of Victoria, P. O. Box 3055, Petch Bldg., Victoria, British Columbia V8W 3P6, Canada

The MgCl2-induced folding of defined 12-mer nucleosomal arrays, in which ubiquitinated histone H2A (uH2A) replaced H2A, was analyzed by quantitative agarose gel electrophoresis and analytical centrifugation. Both types of analysis showed that uH2A arrays attained a degree of compaction similar to that of control arrays in 2 mM MgCl2. These results indicate that attachment of ubiquitin to H2A has little effect on the ability of nucleosomal arrays to form higher order folded structures in the ionic conditions tested. In contrast, uH2A arrays were found to oligomerize at lower MgCl2 concentrations than control nucleosomal arrays, suggesting that histone ubiquitination may play a role in nucleosomal fiber association.

* This work was supported by a Foundation for Research Development research grant and a University of Cape Town research fund grant (to G. L.) and by a Medical Research Council of Canada grant (MT-13104 to J. A.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Tel.: 27-21-650-4006; Fax: 27-21-685-5931; E-mail: laure@molbiol.uct.ac.za.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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