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J. Biol. Chem., Vol. 282, Issue 45, 32867-32876, November 9, 2007

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Site-specific Binding Affinities within the H2B Tail Domain Indicate Specific Effects of Lysine Acetylation^*

From the Department of Biochemistry and Biophysics, University of Rochester, Rochester, New York 14642

Acetylation of specific lysines within the core histone tail domains plays a critical role in regulating chromatin-based activities. However, the structures and interactions of the tail domains and the molecular mechanisms by which acetylation directly alters chromatin structures are not well understood. To address these issues we developed a chemical method to quantitatively determine binding affinities of specific regions within the individual tail domains in model chromatin complexes. Examinations of specific sites within the H2B tail domain indicate that this tail contains distinct structural elements and binds within nucleosomes with affinities that would reduce the activity of tail-binding proteins 10–50-fold from that deduced from peptide binding studies. Moreover, we find that mutations mimicking lysine acetylation do not cause a global weakening of tail-DNA interactions but rather the results suggest that acetylation leads to a much more subtle and specific alteration in tail interactions than has been assumed. In addition, we provide evidence that acetylation at specific sites in the tail is not additive with several events resulting in similar, localized changes in tail binding.

Received for publication, July 23, 2007 , and in revised form, August 20, 2007.

^* This work was supported by National Institutes of Health Grant GM52426. 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 supplemental Figs. S1 and S2.

¹ To whom correspondence should be addressed. E-mail: Jeffrey_Hayes{at}urmc.rochester.edu.

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