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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
2004-8-18
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pubmed:abstractText |
H2A.Bbd is an unusual histone variant whose sequence is only 48% conserved compared to major H2A. The major sequence differences are in the docking domain that tethers the H2A-H2B dimer to the (H3-H4)(2) tetramer; in addition, the C-terminal tail is absent in H2A.Bbd. We assembled nucleosomes in which H2A is replaced by H2A.Bbd (Bbd-NCP), and found that Bbd-NCP had a more relaxed structure in which only 118+/-2 bp of DNA is protected against digestion with micrococcal nuclease. The absence of fluorescence resonance energy transfer between the ends of the DNA in Bbd-NCP indicates that the distance between the DNA ends is increased significantly. The Bbd docking domain is largely responsible for this behavior, as shown by domain-swap experiments. Bbd-containing nucleosomal arrays repress transcription from a natural promoter, and this repression can be alleviated by transcriptional activators Tax and CREB. The structural properties of Bbd-NCP described here have important implications for the in vivo function of this histone variant and are consistent with its proposed role in transcriptionally active chromatin.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-10638745,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-10666246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-10921904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-11101893,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-11114523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-11266453,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-11739728,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-11850638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-12045097,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-12082075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-12581654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-12660166,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-12672489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-12876341,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-12928440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-12934006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-14583738,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-14608368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-14739929,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-1480489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-14870657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-2223068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-2996776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-3351917,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-728412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-8027077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-8420969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-8649423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-8851972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-9230310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-9305837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-9325091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15257289-9450928
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3314-24
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pubmed:dateRevised |
2011-8-5
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pubmed:meshHeading |
pubmed-meshheading:15257289-Amino Acid Sequence,
pubmed-meshheading:15257289-Animals,
pubmed-meshheading:15257289-Base Pairing,
pubmed-meshheading:15257289-DNA,
pubmed-meshheading:15257289-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:15257289-Histones,
pubmed-meshheading:15257289-Humans,
pubmed-meshheading:15257289-Micrococcal Nuclease,
pubmed-meshheading:15257289-Models, Molecular,
pubmed-meshheading:15257289-Molecular Sequence Data,
pubmed-meshheading:15257289-Nucleosomes,
pubmed-meshheading:15257289-Oligonucleotide Array Sequence Analysis,
pubmed-meshheading:15257289-Promoter Regions, Genetic,
pubmed-meshheading:15257289-Protein Binding,
pubmed-meshheading:15257289-Protein Conformation,
pubmed-meshheading:15257289-Protein Folding,
pubmed-meshheading:15257289-Sequence Alignment,
pubmed-meshheading:15257289-Transcription, Genetic
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pubmed:year |
2004
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pubmed:articleTitle |
Nucleosomes containing the histone variant H2A.Bbd organize only 118 base pairs of DNA.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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