Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B

M. E. Nemergut, C. A. Mizzen, T. Stukenberg, C. D. Allis, I. G. Macara

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)1540-1543
Number of pages4
JournalScience
Volume292
Issue number5521
DOIs
StatePublished - May 25 2001

ASJC Scopus subject areas

  • General

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    Nemergut, M. E., Mizzen, C. A., Stukenberg, T., Allis, C. D., & Macara, I. G. (2001). Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B. Science, 292(5521), 1540-1543. https://doi.org/10.1126/science.292.5521.1540