Source:http://linkedlifedata.com/resource/pubmed/id/16580668
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2006-4-17
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pubmed:abstractText |
To start to understand the role of chromatin structure in regulating transcription in trypanosomes, we analyzed covalent modifications on the four core histones of Trypanosoma brucei. We found unusually few modifications in the N-terminal tails, which are abundantly modified in other organisms and whose sequences, but not composition, are highly divergent in trypanosomes. In contrast, the C-terminal region of H2A appears to be hyper-acetylated. Surprisingly, the N-terminal alanines of H2A, H2B, and H4, were mono-methylated, a modification that has not been described previously for histones. Possible functions and evolutionary explanations for these unusual histone modifications are discussed.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
580
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2306-10
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16580668-Acetylation,
pubmed-meshheading:16580668-Animals,
pubmed-meshheading:16580668-Chromatin,
pubmed-meshheading:16580668-Evolution, Molecular,
pubmed-meshheading:16580668-Gene Expression Regulation,
pubmed-meshheading:16580668-Histones,
pubmed-meshheading:16580668-Methylation,
pubmed-meshheading:16580668-Protein Processing, Post-Translational,
pubmed-meshheading:16580668-Protozoan Proteins,
pubmed-meshheading:16580668-Trypanosoma brucei brucei
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pubmed:year |
2006
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pubmed:articleTitle |
Unusual histone modifications in Trypanosoma brucei.
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pubmed:affiliation |
Laboratory of Molecular Parasitology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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