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Function of multiple Lis-Homology domain/WD-40 repeat-containing proteins in feed-forward transcriptional repression by silencing mediator for retinoic and thyroid receptor/nuclear receptor corepressor complexes

DC FieldValueLanguage
dc.contributor.author강희범-
dc.contributor.author김한천-
dc.contributor.author윤호근-
dc.contributor.author이유현-
dc.contributor.author최경철-
dc.contributor.author최효경-
dc.date.accessioned2015-05-19T16:45:43Z-
dc.date.available2015-05-19T16:45:43Z-
dc.date.issued2008-
dc.identifier.issn0888-8809-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/106896-
dc.description.abstractLis-homology (LisH) motifs are involved in protein dimerization, and the discovery of the conserved N-terminal LisH domain in transducin beta-like protein 1 and its receptor (TBL1 and TBLR1) led us to examine the role of this domain in transcriptional repression. Here we show that multiple beta-transducin (WD-40) repeat-containing proteins interact to form oligomers in solution and that oligomerization depends on the presence of the LisH domain in each protein. Repression of transcription, as assayed using Gal4 fusion proteins, also depended on the presence of the LisH domain, suggesting that oligomerization is a prerequisite for efficient transcriptional repression. Furthermore, we show that the LisH domain is responsible for the binding to the hypoacetylated histone H4 tail and for stable chromatin targeting by the nuclear receptor corepressor complex. Mutations in conserved residues in the LisH motif of TBL1 and TBLR1 block histone binding, oligomerization, and transcriptional repression, supporting the functional importance of the LisH motif in transcriptional repression. Our results indicate that another WD-40 protein, TBL3, also preferentially binds to the N-terminal domain of TBL1 and TBLR1, and forms oligomers with other WD-40 proteins. Finally, we observed that the WD-40 proteins RbAp46 and RbAp48 of the sin3A corepressor complex failed to dimerize. We also found the specific interaction UbcH/E2 with TBL1, but not RbAp46/48. Altogether, our results thus indicate that the presence of multiple LisH/WD-40 repeat containing proteins is exclusive to nuclear receptor corepressor/ silencing mediator for retinoic and thyroid receptor complexes compared with other class 1 histone deacetylase-containing corepessor complexes-
dc.description.statementOfResponsibilityopen-
dc.format.extent1093~1104-
dc.relation.isPartOfMOLECULAR ENDOCRINOLOGY-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.subject.MESHAmino Acid Motifs/genetics-
dc.subject.MESHAmino Acid Sequence-
dc.subject.MESHBinding Sites/genetics-
dc.subject.MESHBlotting, Western-
dc.subject.MESHCell Line-
dc.subject.MESHChromatin/metabolism-
dc.subject.MESHChromatin Immunoprecipitation-
dc.subject.MESHDNA Mutational Analysis-
dc.subject.MESHHeLa Cells-
dc.subject.MESHHistones/metabolism-
dc.subject.MESHHumans-
dc.subject.MESHImmunoprecipitation-
dc.subject.MESHNuclear Proteins/genetics-
dc.subject.MESHNuclear Proteins/metabolism*-
dc.subject.MESHNuclear Receptor Co-Repressor 1-
dc.subject.MESHProtein Binding-
dc.subject.MESHReceptors, Retinoic Acid/genetics-
dc.subject.MESHReceptors, Retinoic Acid/metabolism*-
dc.subject.MESHReceptors, Thyroid Hormone/genetics-
dc.subject.MESHReceptors, Thyroid Hormone/metabolism*-
dc.subject.MESHRepetitive Sequences, Amino Acid/genetics-
dc.subject.MESHRepressor Proteins/genetics-
dc.subject.MESHRepressor Proteins/metabolism*-
dc.subject.MESHReverse Transcriptase Polymerase Chain Reaction-
dc.subject.MESHSequence Homology, Amino Acid-
dc.subject.MESHTranscription, Genetic*-
dc.titleFunction of multiple Lis-Homology domain/WD-40 repeat-containing proteins in feed-forward transcriptional repression by silencing mediator for retinoic and thyroid receptor/nuclear receptor corepressor complexes-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentDept. of Biochemistry & Molecular Biology (생화학,분자생물학)-
dc.contributor.googleauthorHyo-Kyoung Choi-
dc.contributor.googleauthorKyung-Chul Choi-
dc.contributor.googleauthorHee-Bum Kang-
dc.contributor.googleauthorHan-Cheon Kim-
dc.contributor.googleauthorYoo-Hyun Lee-
dc.contributor.googleauthorSeungjoo Haam, Hyoung-Gi Park-
dc.contributor.googleauthorHo-Geun Yoon-
dc.identifier.doi10.1210/me.2007-0396-
dc.admin.authorfalse-
dc.admin.mappingfalse-
dc.contributor.localIdA00103-
dc.contributor.localIdA01103-
dc.contributor.localIdA02625-
dc.contributor.localIdA03017-
dc.contributor.localIdA04035-
dc.contributor.localIdA04225-
dc.relation.journalcodeJ02257-
dc.identifier.eissn1944-9917-
dc.identifier.pmid18202150-
dc.identifier.urlhttp://press.endocrine.org/doi/abs/10.1210/me.2007-0396-
dc.subject.keywordAmino Acid Motifs/genetics-
dc.subject.keywordAmino Acid Sequence-
dc.subject.keywordBinding Sites/genetics-
dc.subject.keywordBlotting, Western-
dc.subject.keywordCell Line-
dc.subject.keywordChromatin/metabolism-
dc.subject.keywordChromatin Immunoprecipitation-
dc.subject.keywordDNA Mutational Analysis-
dc.subject.keywordHeLa Cells-
dc.subject.keywordHistones/metabolism-
dc.subject.keywordHumans-
dc.subject.keywordImmunoprecipitation-
dc.subject.keywordNuclear Proteins/genetics-
dc.subject.keywordNuclear Proteins/metabolism*-
dc.subject.keywordNuclear Receptor Co-Repressor 1-
dc.subject.keywordProtein Binding-
dc.subject.keywordReceptors, Retinoic Acid/genetics-
dc.subject.keywordReceptors, Retinoic Acid/metabolism*-
dc.subject.keywordReceptors, Thyroid Hormone/genetics-
dc.subject.keywordReceptors, Thyroid Hormone/metabolism*-
dc.subject.keywordRepetitive Sequences, Amino Acid/genetics-
dc.subject.keywordRepressor Proteins/genetics-
dc.subject.keywordRepressor Proteins/metabolism*-
dc.subject.keywordReverse Transcriptase Polymerase Chain Reaction-
dc.subject.keywordSequence Homology, Amino Acid-
dc.subject.keywordTranscription, Genetic*-
dc.contributor.alternativeNameKang, Hee Bum-
dc.contributor.alternativeNameKim, Han Cheon-
dc.contributor.alternativeNameYoon, Ho Geun-
dc.contributor.alternativeNameLee, Yoo Hyun-
dc.contributor.alternativeNameChoi, Kyung Chul-
dc.contributor.alternativeNameChoi, Hyo Kyoung-
dc.contributor.affiliatedAuthorKang, Hee Bum-
dc.contributor.affiliatedAuthorKim, Han Cheon-
dc.contributor.affiliatedAuthorYoon, Ho Geun-
dc.contributor.affiliatedAuthorLee, Yoo Hyun-
dc.contributor.affiliatedAuthorChoi, Kyung Chul-
dc.contributor.affiliatedAuthorChoi, Hyo Kyoung-
dc.rights.accessRightsnot free-
dc.citation.volume22-
dc.citation.number5-
dc.citation.startPage1093-
dc.citation.endPage1104-
dc.identifier.bibliographicCitationMOLECULAR ENDOCRINOLOGY , Vol.22(5) : 1093-1104, 2008-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Biochemistry and Molecular Biology (생화학-분자생물학교실) > 1. Journal Papers

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