Source:http://linkedlifedata.com/resource/pubmed/id/21111233
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2010-11-29
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pubmed:databankReference | |
pubmed:abstractText |
Histone variant H2A.Z-containing nucleosomes are incorporated at most eukaryotic promoters. This incorporation is mediated by the conserved SWR1 complex, which replaces histone H2A in canonical nucleosomes with H2A.Z in an ATP-dependent manner. Here, we show that promoter-proximal nucleosomes are highly heterogeneous for H2A.Z in Saccharomyces cerevisiae, with substantial representation of nucleosomes containing one, two, or zero H2A.Z molecules. SWR1-catalyzed H2A.Z replacement in vitro occurs in a stepwise and unidirectional fashion, one H2A.Z-H2B dimer at a time, producing heterotypic nucleosomes as intermediates and homotypic H2A.Z nucleosomes as end products. The ATPase activity of SWR1 is specifically stimulated by H2A-containing nucleosomes without ensuing histone H2A eviction. Remarkably, further addition of free H2A.Z-H2B dimer leads to hyperstimulation of ATPase activity, eviction of nucleosomal H2A-H2B, and deposition of H2A.Z-H2B. These results suggest that the combination of H2A-containing nucleosome and free H2A.Z-H2B dimer acting as both effector and substrate for SWR1 governs the specificity and outcome of the replacement reaction.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Swr1 protein, S cerevisiae
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1097-4172
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
24
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pubmed:volume |
143
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
725-36
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pubmed:meshHeading |
pubmed-meshheading:21111233-Adenosine Triphosphatases,
pubmed-meshheading:21111233-Chromatin Assembly and Disassembly,
pubmed-meshheading:21111233-Dimerization,
pubmed-meshheading:21111233-Histones,
pubmed-meshheading:21111233-Nucleosomes,
pubmed-meshheading:21111233-Promoter Regions, Genetic,
pubmed-meshheading:21111233-Saccharomyces cerevisiae,
pubmed-meshheading:21111233-Saccharomyces cerevisiae Proteins
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pubmed:year |
2010
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pubmed:articleTitle |
Stepwise histone replacement by SWR1 requires dual activation with histone H2A.Z and canonical nucleosome.
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pubmed:affiliation |
Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. luked@mail.nih.gov
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Intramural
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