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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2005-6-27
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pubmed:abstractText |
CENP-A is an essential histone H3 variant found in all eukaryotes examined to date. To begin to determine how CENP-A is assembled into chromatin, we developed a binding assay using sperm chromatin in cell-free extract derived from Xenopus eggs. Our data suggest that the catalytic activities of an unidentified deoxycytidine deaminase and UNG2, a uracil DNA glycosylase, are involved in CENP-A assembly. In support of this model, inhibiting deoxycytidine deaminase with zebularine, or uracil DNA glycosylase with Ugi, uracil or UTP results in a lack of detectable CENP-A on sperm DNA. Conversely, inducing DNA damage increases the level of CENP-A detected on sperm chromatin. Our data suggest that base excision repair may be involved in assembly of this histone H3 variant.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Glycosylases,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside Deaminases,
http://linkedlifedata.com/resource/pubmed/chemical/Uracil,
http://linkedlifedata.com/resource/pubmed/chemical/Uracil-DNA Glycosidase,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/centromere protein A,
http://linkedlifedata.com/resource/pubmed/chemical/deoxycytidine deaminase
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1568-7864
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
760-72
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15964249-Amino Acid Sequence,
pubmed-meshheading:15964249-Animals,
pubmed-meshheading:15964249-Autoantigens,
pubmed-meshheading:15964249-Catalysis,
pubmed-meshheading:15964249-Cell Nucleus,
pubmed-meshheading:15964249-Chromatin,
pubmed-meshheading:15964249-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:15964249-DNA Damage,
pubmed-meshheading:15964249-DNA Glycosylases,
pubmed-meshheading:15964249-DNA Repair,
pubmed-meshheading:15964249-DNA Replication,
pubmed-meshheading:15964249-Female,
pubmed-meshheading:15964249-G2 Phase,
pubmed-meshheading:15964249-Male,
pubmed-meshheading:15964249-Molecular Sequence Data,
pubmed-meshheading:15964249-Nucleoside Deaminases,
pubmed-meshheading:15964249-Ovum,
pubmed-meshheading:15964249-Spermatozoa,
pubmed-meshheading:15964249-Uracil,
pubmed-meshheading:15964249-Uracil-DNA Glycosidase,
pubmed-meshheading:15964249-Xenopus Proteins,
pubmed-meshheading:15964249-Xenopus laevis
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pubmed:year |
2005
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pubmed:articleTitle |
Xenopus CENP-A assembly into chromatin requires base excision repair proteins.
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pubmed:affiliation |
Department of Biological Sciences, University of California San Diego, Mail Code 0322, La Jolla, CA 92093, USA. szeitlin@biomail.ucsd.edu
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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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