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PMID: 11375490 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

Science (New York, N.Y.) ·Vol. 292 ·No. 5521 ·2001-05-25 ·Pages 1540-3

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.

MeSH Terms

Active Transport, Cell Nucleus Animals Catalysis Cell Cycle Proteins Cell Nucleus/metabolism Chickens Chromatin/metabolism DNA/metabolism DNA-Binding Proteins/metabolism Dimerization Guanine Nucleotide Exchange Factors Guanosine Diphosphate/metabolism Guanosine Triphosphate/metabolism HeLa Cells Histones/metabolism Humans Male Nuclear Envelope/metabolism Nuclear Proteins Nucleosomes/metabolism Recombinant Fusion Proteins/metabolism Spermatozoa Xenopus Proteins Xenopus laevis ran GTP-Binding Protein/metabolism

Chemicals

Cell Cycle Proteins Chromatin DNA-Binding Proteins Guanine Nucleotide Exchange Factors Histones Nuclear Proteins Nucleosomes RCC1 protein, Xenopus RCC1 protein, human Recombinant Fusion Proteins Xenopus Proteins Guanosine Diphosphate Guanosine Triphosphate DNA ran GTP-Binding Protein

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Nemergut M E

Center for Cell Signaling, University of Virginia, Charlottesville, VA 22908, USA. [email protected]

Mizzen C A

Stukenberg T

Allis C D

Macara I G

Article Info

Journal

Science (New York, N.Y.)

Abbr.

Science

ISSN

0036-8075

DOI

10.1126/science.292.5521.1540

[email protected]

Published

2001-05-25

Pages

1540-3

Language

English

Region

United States

NLM ID

0404511

Subset

Grants

NIGMS NIH HHS · GM-50526 · United States

External Links

PubMed source DOI: 10.1126/science.292.5521.1540 View journal details

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

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