| Chz1, a nuclear chaperone for histone H2AZ. | |
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MedLine Citation:
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PMID: 17289584 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The histone variant H2AZ marks nucleosomes flanking the promoters of most genes of budding yeast. The incorporation of H2AZ into chromatin is dependent on the SWR1 complex, which catalyses the replacement of conventional histone H2A with H2AZ. In cells, the pool of unincorporated histone H2AZ has previously been found in association with Nap1, a chaperone for conventional histone H2A-H2B. Here, we report the discovery of Chz1, a histone chaperone that has preference for H2AZ and can also deliver a source of the histone variant for SWR1-dependent histone replacement. Bacterially expressed Chz1 forms a heterotrimer with H2AZ-H2B, stabilizing the association of the histone dimer. We have identified a conserved motif important for histone variant recognition within the H2AZ-interacting domain of Chz1. The presence of this motif in other metazoan proteins suggests that H2AZ-specific chaperones may be widely conserved. |
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Authors:
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Ed Luk; Ngoc-Diep Vu; Kem Patteson; Gaku Mizuguchi; Wei-Hua Wu; Anand Ranjan; Jonathon Backus; Subhojit Sen; Marc Lewis; Yawen Bai; Carl Wu |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Intramural |
Journal Detail:
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Title: Molecular cell Volume: 25 ISSN: 1097-2765 ISO Abbreviation: Mol. Cell Publication Date: 2007 Feb |
Date Detail:
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Created Date: 2007-02-09 Completed Date: 2007-03-27 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 9802571 Medline TA: Mol Cell Country: United States |
Other Details:
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Languages: eng Pagination: 357-68 Citation Subset: IM |
Affiliation:
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Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. luked@mail.nih.gov |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphatases
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metabolism Amino Acid Sequence Carrier Proteins / chemistry Cell Cycle Proteins / physiology Conserved Sequence Dimerization Histone Chaperones Histones / metabolism* Humans Molecular Chaperones / chemistry, metabolism, physiology* Molecular Sequence Data Nuclear Proteins / physiology Nucleosome Assembly Protein 1 Saccharomyces cerevisiae / genetics, metabolism* Saccharomyces cerevisiae Proteins / chemistry, metabolism, physiology* Sequence Alignment |
| Chemical | |
Reg. No./Substance:
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0/Carrier Proteins; 0/Cell Cycle Proteins; 0/Chz1 protein, S cerevisiae; 0/HIRIP3 protein, human; 0/Histone Chaperones; 0/Histones; 0/Htz1 protein, S cerevisiae; 0/Molecular Chaperones; 0/NAP1 protein, S cerevisiae; 0/NAP1L1 protein, human; 0/Nuclear Proteins; 0/Nucleosome Assembly Protein 1; 0/Saccharomyces cerevisiae Proteins; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.3/Swr1 protein, S cerevisiae |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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