pubmed-article:8280071 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8280071 | lifeskim:mentions | umls-concept:C0028623 | lld:lifeskim |
pubmed-article:8280071 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:8280071 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
pubmed-article:8280071 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
pubmed-article:8280071 | lifeskim:mentions | umls-concept:C1156200 | lld:lifeskim |
pubmed-article:8280071 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
pubmed-article:8280071 | pubmed:dateCreated | 1994-2-7 | lld:pubmed |
pubmed-article:8280071 | pubmed:abstractText | The properties of the nucleosomes of a salt-soluble, transcriptionally active gene-enriched fraction of chicken erythrocyte chromatin were evaluated by hydroxyapatite dissociation chromatography. We have demonstrated previously that the salt-soluble, transcriptionally active gene-enriched polynucleosomes are enriched in dynamically acetylated and ubiquitinated histones, and in an atypical U-shaped nucleosome that possessed about 20% less protein than a typical nucleosome. Further, newly synthesized histones H2A and H2B exchange preferentially with the nucleosomal histones H2A and H2B of this salt-soluble chromatin fraction. Analysis of the histones eluting from the hydroxyapatite-bound chromatin demonstrated that hyperacetylated and ubiquitinated (u), including multi-ubiquitinated, H2A-H2B.1 dimers dissociated at lower concentrations of NaCl than unmodified dimers or dimers with histone variants H2A.Z and/or H2B.2. Cross-linking studies revealed that at least 50% of uH2B.1 was paired with uH2A. uH2A-uH2B.1 dimers dissociated at lower NaCl concentrations than H2A-uH2B.1 dimers. Hyperacetylated histone (H3-H4)2 tetramers also eluted at lower concentrations of NaCl than unmodified tetramers. Our results support the idea that acetylation and ubiquitination of histones H2A and H2B.1 increase the lability of H2A-H2B.1 dimers in transcriptionally active nucleosomes. In contrast, our observations suggest that histone variants H2A.Z and H2B.2. stabilize the association of the H2A-H2B dimer in nucleosomes. The elevated lability of the H2A-H2B dimer may facilitate processes such as the exchange of these dimers with newly synthesized histones, the elongation process of transcription and transcription factor binding. | lld:pubmed |
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pubmed-article:8280071 | pubmed:language | eng | lld:pubmed |
pubmed-article:8280071 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8280071 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8280071 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8280071 | pubmed:month | Dec | lld:pubmed |
pubmed-article:8280071 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:8280071 | pubmed:author | pubmed-author:DavidJ SJS | lld:pubmed |
pubmed-article:8280071 | pubmed:author | pubmed-author:LUCC | lld:pubmed |
pubmed-article:8280071 | pubmed:author | pubmed-author:HendzelM JMJ | lld:pubmed |
pubmed-article:8280071 | pubmed:author | pubmed-author:DelcuveG PGP | lld:pubmed |
pubmed-article:8280071 | pubmed:author | pubmed-author:NagarajaSS | lld:pubmed |
pubmed-article:8280071 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8280071 | pubmed:day | 15 | lld:pubmed |
pubmed-article:8280071 | pubmed:volume | 296 ( Pt 3) | lld:pubmed |
pubmed-article:8280071 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8280071 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8280071 | pubmed:pagination | 737-44 | lld:pubmed |
pubmed-article:8280071 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:8280071 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8280071 | pubmed:articleTitle | Effects of histone acetylation, ubiquitination and variants on nucleosome stability. | lld:pubmed |
pubmed-article:8280071 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Manitoba, Winnipeg, Canada. | lld:pubmed |
pubmed-article:8280071 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8280071 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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