|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
3
|
|
pubmed:dateCreated |
2003-2-26
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Site-specific lysine methylation of histones by SET domains is a hallmark for epigenetic control of gene transcription in eukaryotic organisms. Here we report that a SET domain protein from Paramecium bursaria chlorella virus can specifically di-methylate Lys27 in histone H3, a modification implicated in gene silencing. The solution structure of the viral SET domain reveals a butterfly-shaped head-to-head symmetric dimer different from other known protein methyltransferases. Each subunit consists of a Greek-key antiparallel beta-barrel and a three-stranded open-faced sandwich that mediates the dimer interface. Cofactor S-adenosyl-L-methionine (SAM) binds at the opening of the beta-barrel, and amino acids C-terminal to Lys27 in H3 and in the flexible C-terminal tail of the enzyme confer the specificity of this viral histone methyltransferase.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Mar
|
|
pubmed:issn |
1072-8368
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
10
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
187-96
|
|
pubmed:dateRevised |
2008-11-21
|
|
pubmed:meshHeading |
pubmed-meshheading:12567185-Amino Acid Sequence,
pubmed-meshheading:12567185-Animals,
pubmed-meshheading:12567185-Binding Sites,
pubmed-meshheading:12567185-Dimerization,
pubmed-meshheading:12567185-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:12567185-Histones,
pubmed-meshheading:12567185-Lysine,
pubmed-meshheading:12567185-Methylation,
pubmed-meshheading:12567185-Methyltransferases,
pubmed-meshheading:12567185-Models, Molecular,
pubmed-meshheading:12567185-Molecular Sequence Data,
pubmed-meshheading:12567185-Mutagenesis,
pubmed-meshheading:12567185-Paramecium,
pubmed-meshheading:12567185-Phycodnaviridae,
pubmed-meshheading:12567185-Protein Conformation,
pubmed-meshheading:12567185-Protein Methyltransferases,
pubmed-meshheading:12567185-Protein Structure, Tertiary,
pubmed-meshheading:12567185-S-Adenosylmethionine,
pubmed-meshheading:12567185-Sequence Homology, Amino Acid,
pubmed-meshheading:12567185-Structural Homology, Protein,
pubmed-meshheading:12567185-Substrate Specificity,
pubmed-meshheading:12567185-Viral Proteins
|
|
pubmed:year |
2003
|
|
pubmed:articleTitle |
A dimeric viral SET domain methyltransferase specific to Lys27 of histone H3.
|
|
pubmed:affiliation |
Structural Biology Program, Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York University, One Gustave L. Levy Place, New York, New York 10029, USA.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
