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Science 25 May 2001:
Vol. 292. no. 5521, pp. 1540 - 1543
DOI: 10.1126/science.292.5521.1540
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Reports

Chromatin Docking and Exchange Activity Enhancement of RCC1 by Histones H2A and H2B

Michael E. Nemergut,12*dagger Craig A. Mizzen,4 Todd Stukenberg,4 C. David Allis,4 Ian G. Macara13

The Ran guanosine triphosphatase (GTPase) controls nucleocytoplasmic transport, mitotic spindle formation, and nuclear envelope assembly. These functions rely on the association of the Ran-specific exchange factor, RCC1 (regulator of chromosome condensation 1), with chromatin. We find that RCC1 binds directly to mononucleosomes and to histones H2A and H2B. RCC1 utilizes these histones to bind Xenopus sperm chromatin, and the binding of RCC1 to nucleosomes or histones stimulates the catalytic activity of RCC1. We propose that the docking of RCC1 to H2A/H2B establishes the polarity of the Ran-GTP gradient that drives nuclear envelope assembly, nuclear transport, and other nuclear events.

1 Center for Cell Signaling,
2 Department of Microbiology,
3 Department of Pharmacology,
4 Department of Biochemistry, University of Virginia, Charlottesville, VA 22908, USA.
*   To whom correspondence should be addressed. E-mail: men5w{at}virginia.edu

dagger    Present address: University of Virginia, Hospital West RM 7191, Post Office Box 800577 HSC, Charlottesville, VA 22908.

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