Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2005-10-5
pubmed:abstractText
The replacement histone H2A.Z is variously reported as being linked to gene expression and preventing the spread of heterochromatin in yeast, or concentrated at heterochromatin in mammals. To resolve this apparent dichotomy, affinity-purified antibodies against the N-terminal region of H2A.Z, in both a triacetylated and non-acetylated state, are used in native chromatin immmuno-precipitation experiments with mononucleosomes from three chicken cell types. The hyperacetylated species concentrates at the 5' end of active genes, both tissue specific and housekeeping but is absent from inactive genes, while the unacetylated form is absent from both active and inactive genes. A concentration of H2A.Z is also found at insulators under circumstances implying a link to barrier activity but not to enhancer blocking. Although acetylated H2A.Z is widespread throughout the interphase genome, at mitosis its acetylation is erased, the unmodified form remaining. Thus, although H2A.Z may operate as an epigenetic marker for active genes, its N-terminal acetylation does not.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-10220430, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-10406808, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-10811622, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-11081628, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-11090616, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-11274167, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-11331588, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-11498546, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-11516949, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-11788708, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-11893489, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-12628191, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-12660166, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-12865423, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-12963728, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-14645854, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-14661024, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-14690608, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-14759373, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-14966270, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-15195148, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-15196461, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-15485911, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-15616580, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-15878876, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-2893693, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-7418000, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-8168481, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-8348617, http://linkedlifedata.com/resource/pubmed/commentcorrection/16204459-9334168
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1362-4962
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5633-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken.
pubmed:affiliation
Biophysics Laboratories, Institute of Biomedical and Biomolecular Sciences, Faculty of Science, University of Portsmouth, Portsmouth, PO1 2DT, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't