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Molecular and Cellular Biology, February 2001, p. 875-883, Vol. 21, No. 3
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.3.875-883.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Critical Role for the Histone H4 N Terminus in Nucleosome Remodeling by ISWI

Cedric R. Clapier,1,2 Gernot Längst,1 Davide F. V. Corona,2 Peter B. Becker,1,* and Karl P. Nightingale3

Adolf Butenandt-Institut, Molekularbiologie, Ludwig-Maximilians-Universität München, 80336 Munich,1 and International Ph.D. Programme of the European Molecular Biology Laboratory, 69117 Heidelberg,2 Germany, and Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom3

Received 1 August 2000/Returned for modification 6 September 2000/Accepted 1 November 2000

The ATPase ISWI can be considered the catalytic core of several multiprotein nucleosome remodeling machines. Alone or in the context of nucleosome remodeling factor, the chromatin accessibility complex (CHRAC), or ACF, ISWI catalyzes a number of ATP-dependent transitions of chromatin structure that are currently best explained by its ability to induce nucleosome sliding. In addition, ISWI can function as a nucleosome spacing factor during chromatin assembly, where it will trigger the ordering of newly assembled nucleosomes into regular arrays. Both nucleosome remodeling and nucleosome spacing reactions are mechanistically unexplained. As a step toward defining the interaction of ISWI with its substrate during nucleosome remodeling and chromatin assembly we generated a set of nucleosomes lacking individual histone N termini from recombinant histones. We found the conserved N termini (the N-terminal tails) of histone H4 essential to stimulate ISWI ATPase activity, in contrast to other histone tails. Remarkably, the H4 N terminus, but none of the other tails, was critical for CHRAC-induced nucleosome sliding and for the generation of regularity in nucleosomal arrays by ISWI. Direct nucleosome binding studies did not reflect a dependence on the H4 tail for ISWI-nucleosome interactions. We conclude that the H4 tail is critically required for nucleosome remodeling and spacing at a step subsequent to interaction with the substrate.

* Corresponding author. Mailing address: Adolf Butenandt-Institut, Molekularbiologie, Schillerstr. 44, 80336 Munich, Germany. Phone: 49-89-5996-427 (428). Fax: 49-89-5996-425. E-mail: pbecker{at}mol-bio.med.uni-muenchen.de.

Molecular and Cellular Biology, February 2001, p. 875-883, Vol. 21, No. 3
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.3.875-883.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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