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XB-ART-8988
Science May 25, 2001; 292 (5521): 1540-3.
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Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B.

Nemergut ME , Mizzen CA , Stukenberg T , Allis CD , Macara IG .


Abstract
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.

PubMed ID: 11375490
Article link: Science
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: h2ac21 h2bc21 ran rcc1