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Structure and Function of Histone H3 Lysine 9 Methyltransferases and Demethylases

dc.contributor.authorKrishnan , Swathien_US
dc.contributor.authorHorowitz , Scotten_US
dc.contributor.authorTrievel, Raymond C.en_US
dc.date.accessioned2011-02-02T18:00:21Z
dc.date.available2012-02-21T18:47:01Zen_US
dc.date.issued2011-01-24en_US
dc.identifier.citationKrishnan , Swathi; Horowitz , Scott; Trievel, Raymond C. (2011). "Structure and Function of Histone H3 Lysine 9 Methyltransferases and Demethylases." ChemBioChem 12(2): 254-263. <http://hdl.handle.net/2027.42/79431>en_US
dc.identifier.issn1439-4227en_US
dc.identifier.issn1439-7633en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/79431
dc.description.abstractHistone lysine methylation is a dynamic chromatin modification that plays key regulatory roles in gene expression and other genomic functions. Methylation of Lys9 in histone H3 (H3K9) is a prominent modification that has been implicated in diverse processes, including transcriptional silencing, heterochromatin formation, and DNA methylation. In this review, we summarize recent advances in understanding the structure and substrate specificity of the H3K9-specific methyltransferases G9A and GLP and explore current efforts to develop inhibitors of these enzymes. In addition, we discuss the structure and specificity of the recently discovered PHF8 family of histone demethylases that target H3K9 as well as other methylation sites in histones H3 and H4. Finally, we conclude by comparing the H3K9 binding modes displayed by these enzymes and examine the relevance of these studies to their biological functions and to structure-based inhibitor design.en_US
dc.format.extent834283 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherWILEY-VCH Verlagen_US
dc.subject.otherChemistryen_US
dc.subject.otherBiochemistry and Biotechnologyen_US
dc.titleStructure and Function of Histone H3 Lysine 9 Methyltransferases and Demethylasesen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumUniversity of Michigan Medical School, Department of Biological Chemistry, 1150 West Medical Center Drive, 4315 Medical Science Research Building III, Ann Arbor, MI 48109 (USA) ; These authors contributed equally to this work.en_US
dc.contributor.affiliationumUniversity of Michigan, Biophysics Graduate Program, Ann Arbor, MI 48109 (USA)en_US
dc.contributor.affiliationumUniversity of Michigan Medical School, Department of Biological Chemistry, 1150 West Medical Center Drive, 5301 Medical Science Research Building III, Ann Arbor, MI 48109 (USA), Fax: (+1) 734-763-4581 ; University of Michigan Medical School, Department of Biological Chemistry, 1150 West Medical Center Drive, 5301 Medical Science Research Building III, Ann Arbor, MI 48109 (USA), Fax: (+1) 734-763-4581en_US
dc.identifier.pmid21243713en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/79431/1/254_ftp.pdf
dc.identifier.doi10.1002/cbic.201000545en_US
dc.identifier.sourceChemBioChemen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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