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Originally published in Science Express on 26 November 2003
Science 16 January 2004:
Vol. 303. no. 5656, pp. 343 - 348
DOI: 10.1126/science.1090701
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Research Articles

ATP-Driven Exchange of Histone H2AZ Variant Catalyzed by SWR1 Chromatin Remodeling Complex

Gaku Mizuguchi,* Xuetong Shen,*{dagger} Joe Landry,* Wei-Hua Wu,{ddagger} Subhojit Sen,{ddagger} Carl Wu§

The conserved histone variant H2AZ has an important role in the regulation of gene expression and the establishment of a buffer to the spread of silent heterochromatin. How histone variants such as H2AZ are incorporated into nucleosomes has been obscure. We have found that Swr1, a Swi2/Snf2-related adenosine triphosphatase, is the catalytic core of a multisubunit, histone-variant exchanger that efficiently replaces conventional histone H2A with histone H2AZ in nucleosome arrays. Swr1 is required for the deposition of histone H2AZ at specific chromosome locations in vivo, and Swr1 and H2AZ commonly regulate a subset of yeast genes. These findings define a previously unknown role for the adenosine triphosphate–dependent chromatin remodeling machinery.

Laboratory of Molecular Cell Biology, National Cancer Institute, National Institutes of Health, Building 37, Room 6068, Bethesda, MD 20892–4255, USA.



Note added in proof: The subunits of the SWR1 complex—Vps72, Swc1, God1, Aor1, and Vps71— have been renamed Swc2, Swc3, Swc4, Swc5, and Swc6, respectively, by agreement with the laboratories of J. Greenblatt, H. Madhani, and J. Rine.

* These authors contributed equally to this work.

{dagger} Present address: Department of Carcinogenesis, MD Anderson Cancer Center, Science Park Research Division, Smithville, TX 78957, USA.

{ddagger} These authors contributed equally to this work.

§ To whom correspondence should be addressed. E-mail: carlwu{at}helix.nih.gov

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Histone H2AZ dimerizes with a novel variant H2B and is enriched at repetitive DNA in Trypanosoma brucei.
J. E. Lowell, F. Kaiser, C. J. Janzen, and G. A. M. Cross (2005)
J. Cell Sci. 118, 5721-5730
   Abstract »    Full Text »    PDF »
Assembly and Disassembly of Nucleosome Core Particles Containing Histone Variants by Human Nucleosome Assembly Protein I.
M. Okuwaki, K. Kato, H. Shimahara, S.-i. Tate, and K. Nagata (2005)
Mol. Cell. Biol. 25, 10639-10651
   Abstract »    Full Text »    PDF »
A Decade of Histone Acetylation: Marking Eukaryotic Chromosomes with Specific Codes.
A. Kimura, K. Matsubara, and M. Horikoshi (2005)
J. Biochem. 138, 647-662
   Abstract »    Full Text »    PDF »
Nuclear Actin-Related Proteins as Epigenetic Regulators of Development.
R. B. Meagher, R. B. Deal, M. K. Kandasamy, and E. C. McKinney (2005)
Plant Physiology 139, 1576-1585
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Two Distinct Mechanisms of Chromatin Interaction by the Isw2 Chromatin Remodeling Complex In Vivo.
T. G. Fazzio, M. E. Gelbart, and T. Tsukiyama (2005)
Mol. Cell. Biol. 25, 9165-9174
   Abstract »    Full Text »    PDF »
TFIID and Spt-Ada-Gcn5-Acetyltransferase Functions Probed by Genome-wide Synthetic Genetic Array Analysis Using a Saccharomyces cerevisiae taf9-ts Allele.
E. Milgrom, R. W. West Jr., C. Gao, and W.-C. W. Shen (2005)
Genetics 171, 959-973
   Abstract »    Full Text »    PDF »
Domain-Wide Displacement of Histones by Activated Heat Shock Factor Occurs Independently of Swi/Snf and Is Not Correlated with RNA Polymerase II Density.
J. Zhao, J. Herrera-Diaz, and D. S. Gross (2005)
Mol. Cell. Biol. 25, 8985-8999
   Abstract »    Full Text »    PDF »
NAP1 Modulates Binding of Linker Histone H1 to Chromatin and Induces an Extended Chromatin Fiber Conformation.
J. F. Kepert, J. Mazurkiewicz, G. L. Heuvelman, K. F. Toth, and K. Rippe (2005)
J. Biol. Chem. 280, 34063-34072
   Abstract »    Full Text »    PDF »
The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken.
K. Bruce, F. A. Myers, E. Mantouvalou, P. Lefevre, I. Greaves, C. Bonifer, D. J. Tremethick, A. W. Thorne, and C. Crane-Robinson (2005)
Nucleic Acids Res. 33, 5633-5639
   Abstract »    Full Text »    PDF »
A Time to Grow, a Time to Flower.
N. A. Eckardt (2005)
PLANT CELL 17, 2615-2617
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