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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
2002-7-17
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pubmed:abstractText |
Covalent modifications of histone N-terminal tails play fundamental roles in regulating chromatin structure and function. Extensive studies have established that acetylation of specific lysine residues in the histone tails plays an important role in transcriptional regulation. Besides acetylation, recent studies have revealed that histone methylation also has significant effects on heterochromatin formation and transcriptional regulation. Histone methylation occurs on specific arginine and lysine residues of histones H3 and H4. Thus far, only 2 residues on histone H4 are known to be methylated. While H4-arginine 3 (H4-R3) methylation is mediated by PRMT1, the enzyme(s) responsible for H4-lysine 20 (H4-K20) methylation is not known.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0960-9822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1086-99
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pubmed:dateRevised |
2010-3-23
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pubmed:meshHeading |
pubmed-meshheading:12121615-3T3 Cells,
pubmed-meshheading:12121615-Acetylation,
pubmed-meshheading:12121615-Amino Acid Sequence,
pubmed-meshheading:12121615-Animals,
pubmed-meshheading:12121615-Binding Sites,
pubmed-meshheading:12121615-Cell Cycle,
pubmed-meshheading:12121615-DNA Methylation,
pubmed-meshheading:12121615-Drosophila,
pubmed-meshheading:12121615-Eukaryotic Cells,
pubmed-meshheading:12121615-Heterochromatin,
pubmed-meshheading:12121615-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:12121615-Histones,
pubmed-meshheading:12121615-Humans,
pubmed-meshheading:12121615-Lysine,
pubmed-meshheading:12121615-Mice,
pubmed-meshheading:12121615-Molecular Sequence Data,
pubmed-meshheading:12121615-Nucleosomes,
pubmed-meshheading:12121615-Sequence Homology, Amino Acid,
pubmed-meshheading:12121615-Substrate Specificity
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pubmed:year |
2002
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pubmed:articleTitle |
Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase.
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pubmed:affiliation |
Department of Biochemistry and Biophysics, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, 27599, 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
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