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Article: Structural Insights of the Specificity and Catalysis of a Viral Histone H3 Lysine 27 Methyltransferase

TitleStructural Insights of the Specificity and Catalysis of a Viral Histone H3 Lysine 27 Methyltransferase
Authors
KeywordsSpecies Index: Eukaryota
Paramecium Bursaria Chlorella Virus 1
Issue Date2006
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmb
Citation
Journal Of Molecular Biology, 2006, v. 359 n. 1, p. 86-96 How to Cite?
AbstractSET domain lysine methyltransferases are known to catalyze site and state-specific methylation of lysine residues in histones that is fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. Here we report the three-dimensional solution structure of the SET domain histone lysine methyltransferase (vSET) from Paramecium bursaria chlorella virus 1 bound to cofactor S-adenosyl-l-homocysteine and a histone H3 peptide containing mono-methylated lysine 27. The dimeric structure, mimicking an enzyme/cofactor/substrate complex, yields the structural basis of the substrate specificity and methylation multiplicity of the enzyme. Our results from mutagenesis and enzyme kinetics analyses argue that a general base mechanism is less likely for lysine methylation by SET domains; and that the only invariant active site residue tyrosine 105 in vSET facilitates methyl transfer from cofactor to the substrate lysine by aligning intermolecular interactions in the lysine access channel of the enzyme. © 2006 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91186
ISSN
2015 Impact Factor: 4.517
2015 SCImago Journal Rankings: 3.002
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorQian, Cen_HK
dc.contributor.authorWang, Xen_HK
dc.contributor.authorManzur, Ken_HK
dc.contributor.authorSachchidananden_HK
dc.contributor.authorFarooq, Aen_HK
dc.contributor.authorZeng, Len_HK
dc.contributor.authorWang, Ren_HK
dc.contributor.authorZhou, MMen_HK
dc.date.accessioned2010-09-17T10:14:25Z-
dc.date.available2010-09-17T10:14:25Z-
dc.date.issued2006en_HK
dc.identifier.citationJournal Of Molecular Biology, 2006, v. 359 n. 1, p. 86-96en_HK
dc.identifier.issn0022-2836en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91186-
dc.description.abstractSET domain lysine methyltransferases are known to catalyze site and state-specific methylation of lysine residues in histones that is fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. Here we report the three-dimensional solution structure of the SET domain histone lysine methyltransferase (vSET) from Paramecium bursaria chlorella virus 1 bound to cofactor S-adenosyl-l-homocysteine and a histone H3 peptide containing mono-methylated lysine 27. The dimeric structure, mimicking an enzyme/cofactor/substrate complex, yields the structural basis of the substrate specificity and methylation multiplicity of the enzyme. Our results from mutagenesis and enzyme kinetics analyses argue that a general base mechanism is less likely for lysine methylation by SET domains; and that the only invariant active site residue tyrosine 105 in vSET facilitates methyl transfer from cofactor to the substrate lysine by aligning intermolecular interactions in the lysine access channel of the enzyme. © 2006 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmben_HK
dc.relation.ispartofJournal of Molecular Biologyen_HK
dc.subjectSpecies Index: Eukaryotaen_HK
dc.subjectParamecium Bursaria Chlorella Virus 1en_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshDNA Mutational Analysisen_HK
dc.subject.meshHistone-Lysine N-Methyltransferase - chemistry - genetics - metabolismen_HK
dc.subject.meshHistones - metabolismen_HK
dc.subject.meshLysine - metabolismen_HK
dc.subject.meshMethylationen_HK
dc.subject.meshModels, Molecularen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshMutagenesis, Site-Directeden_HK
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen_HK
dc.subject.meshParamecium - virologyen_HK
dc.subject.meshPeptides - chemistry - genetics - metabolismen_HK
dc.subject.meshPhycodnaviridae - enzymologyen_HK
dc.subject.meshProtein Methyltransferasesen_HK
dc.subject.meshProtein Structure, Quaternaryen_HK
dc.subject.meshS-Adenosylhomocysteine - chemistry - metabolismen_HK
dc.subject.meshSequence Alignmenten_HK
dc.subject.meshViral Proteins - chemistry - genetics - metabolismen_HK
dc.titleStructural Insights of the Specificity and Catalysis of a Viral Histone H3 Lysine 27 Methyltransferaseen_HK
dc.typeArticleen_HK
dc.identifier.emailQian, C:cmqian@hku.hken_HK
dc.identifier.authorityQian, C=rp01371en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jmb.2006.03.006en_HK
dc.identifier.pmid16603186-
dc.identifier.scopuseid_2-s2.0-33646203168en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33646203168&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume359en_HK
dc.identifier.issue1en_HK
dc.identifier.spage86en_HK
dc.identifier.epage96en_HK
dc.identifier.isiWOS:000237663800009-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridQian, C=7202311105en_HK
dc.identifier.scopusauthoridWang, X=7501870078en_HK
dc.identifier.scopusauthoridManzur, K=6506696841en_HK
dc.identifier.scopusauthoridSachchidanand=11440570300en_HK
dc.identifier.scopusauthoridFarooq, A=7007061775en_HK
dc.identifier.scopusauthoridZeng, L=7401904457en_HK
dc.identifier.scopusauthoridWang, R=36071507000en_HK
dc.identifier.scopusauthoridZhou, MM=7403506618en_HK
dc.identifier.citeulike7155321-

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