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Article: Leucine-rich repeat and WD repeat-containing protein 1 is recruited to pericentric heterochromatin by trimethylated lysine 9 of histone H3 and maintains heterochromatin silencing

TitleLeucine-rich repeat and WD repeat-containing protein 1 is recruited to pericentric heterochromatin by trimethylated lysine 9 of histone H3 and maintains heterochromatin silencing
Authors
Issue Date2012
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2012, v. 287 n. 18, p. 15024-15033 How to Cite?
AbstractLrwd1, a protein containing a leucine-rich repeat and aWD40 repeat domain, interacts with the origin replication complex (ORC), a protein complex involved in both initiation of DNA replication and heterochromatin silencing. Lrwd1 and ORC are known to co-purify with repressive histone marks (trimethylated lysine 9 of histone H3 (H3K9me3) and trimethylated lysine 20 of histone H4 (H4K20me3)) and localize to pericentric heterochromatin. However, how the Lrwd1 is recruited to heterochromatin and the functional significance of the localization of Lrwd1 to the heterochromatin are not known. Here, we show that Lrwd1 preferentially binds to trimethylated repressive histone marks in vitro, which is dependent on an intact WD40 domain but independent of ORC proteins. The localization of Lrwd1 and Orc2 at pericentric heterochromatin in mouse cells is lost in cells lacking H3K9me3 but not in cells lacking H4K20me3. In addition, depletion of HP1α has little impact on the localization of Lrwd1 on pericentric heterochromatin. Finally, depletion of Lrwd1 and Orc2 in mouse cells leads to increased transcription of major satellite repeats. These results indicate that the Lrwd1 is recruited to pericentric heterochromatin through binding to H3K9me3 and that the association of Lrwd1 with pericentric heterochromatin is required for heterochromatin silencing and maintenance. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/184147
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChan, KMen_US
dc.contributor.authorZhang, Zen_US
dc.date.accessioned2013-06-25T03:00:21Z-
dc.date.available2013-06-25T03:00:21Z-
dc.date.issued2012en_US
dc.identifier.citationJournal Of Biological Chemistry, 2012, v. 287 n. 18, p. 15024-15033en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/184147-
dc.description.abstractLrwd1, a protein containing a leucine-rich repeat and aWD40 repeat domain, interacts with the origin replication complex (ORC), a protein complex involved in both initiation of DNA replication and heterochromatin silencing. Lrwd1 and ORC are known to co-purify with repressive histone marks (trimethylated lysine 9 of histone H3 (H3K9me3) and trimethylated lysine 20 of histone H4 (H4K20me3)) and localize to pericentric heterochromatin. However, how the Lrwd1 is recruited to heterochromatin and the functional significance of the localization of Lrwd1 to the heterochromatin are not known. Here, we show that Lrwd1 preferentially binds to trimethylated repressive histone marks in vitro, which is dependent on an intact WD40 domain but independent of ORC proteins. The localization of Lrwd1 and Orc2 at pericentric heterochromatin in mouse cells is lost in cells lacking H3K9me3 but not in cells lacking H4K20me3. In addition, depletion of HP1α has little impact on the localization of Lrwd1 on pericentric heterochromatin. Finally, depletion of Lrwd1 and Orc2 in mouse cells leads to increased transcription of major satellite repeats. These results indicate that the Lrwd1 is recruited to pericentric heterochromatin through binding to H3K9me3 and that the association of Lrwd1 with pericentric heterochromatin is required for heterochromatin silencing and maintenance. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCell Lineen_US
dc.subject.meshChromosomal Proteins, Non-Histone - Genetics - Metabolismen_US
dc.subject.meshGene Silencing - Physiologyen_US
dc.subject.meshHeterochromatin - Genetics - Metabolismen_US
dc.subject.meshHistones - Genetics - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshMiceen_US
dc.subject.meshMice, Knockouten_US
dc.subject.meshMicrotubule Proteins - Genetics - Metabolismen_US
dc.subject.meshOrigin Recognition Complex - Genetics - Metabolismen_US
dc.subject.meshProtein Binding - Physiologyen_US
dc.subject.meshTranscription, Genetic - Physiologyen_US
dc.titleLeucine-rich repeat and WD repeat-containing protein 1 is recruited to pericentric heterochromatin by trimethylated lysine 9 of histone H3 and maintains heterochromatin silencingen_US
dc.typeArticleen_US
dc.identifier.emailChan, KM: ming616@graduate.hku.hken_US
dc.identifier.authorityChan, KM=rp01757en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1074/jbc.M111.337980en_US
dc.identifier.pmid22427655-
dc.identifier.scopuseid_2-s2.0-84860378380en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84860378380&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume287en_US
dc.identifier.issue18en_US
dc.identifier.spage15024en_US
dc.identifier.epage15033en_US
dc.identifier.isiWOS:000304003200064-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridChan, KM=8631854500en_US
dc.identifier.scopusauthoridZhang, Z=35239002800en_US

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