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Transcriptional activity of paired homeobox Pax6 is enhanced by histone acetyltransferase Tip60 during mouse retina development

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dc.contributor.authorKim, Chul-Hong-
dc.contributor.authorKim, Jung-Woong-
dc.contributor.authorJang, Sang-Min-
dc.contributor.authorAn, Joo-Hee-
dc.contributor.authorSong, Ki-Hyun-
dc.contributor.authorChoi, Kyung-Hee-
dc.date.available2019-03-09T02:55:47Z-
dc.date.issued2012-08-
dc.identifier.issn0006-291X-
dc.identifier.issn1090-2104-
dc.identifier.urihttps://scholarworks.bwise.kr/cau/handle/2019.sw.cau/15196-
dc.description.abstractPax6 is a member of the Pax family of transcription factors that contains a DNA binding paired-box and homeobox domain. In animals, including humans, Pax6 plays a key role in development, regulating organogenesis of the eye and brain. The current data show that histone acetyltransferase Tip60 physically interacts with Pax6 in developing post-natal day 4 (P4) mouse retinas. We also found that Tip60 binds with paired-domain of Pax6 using its chromo- and zinc-finger-containing regions, and that these protein interactions were needed for the effective full-transcriptional activation of Pax6. Furthermore, among the combinations of Pax6-target gene interactions using its two DNA binding domain, paired- and homeobox domain, Tip60 significantly enhanced the transcriptional activity of Pax6 on the paired-domain binding sequence (P6CON) containing reporter construct (pCON) than other homeo domain and chimera binding containing pP3 and pCON/P3 constructs. Taken together, these results suggest that Tip60 binds with Pax6 and that this physical interaction leads to the full-transcriptional activation of Pax6 during retina development. (C) 2012 Elsevier Inc. All rights reserved.-
dc.format.extent6-
dc.language영어-
dc.language.isoENG-
dc.publisherACADEMIC PRESS INC ELSEVIER SCIENCE-
dc.titleTranscriptional activity of paired homeobox Pax6 is enhanced by histone acetyltransferase Tip60 during mouse retina development-
dc.typeArticle-
dc.identifier.doi10.1016/j.bbrc.2012.06.126-
dc.identifier.bibliographicCitationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.424, no.3, pp 427 - 432-
dc.description.isOpenAccessN-
dc.identifier.wosid000307618800011-
dc.identifier.scopusid2-s2.0-84864777036-
dc.citation.endPage432-
dc.citation.number3-
dc.citation.startPage427-
dc.citation.titleBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.citation.volume424-
dc.type.docTypeArticle-
dc.publisher.location미국-
dc.subject.keywordAuthorPax6-
dc.subject.keywordAuthorTip60-
dc.subject.keywordAuthorRetinogenesis-
dc.subject.keywordAuthorTranscriptional regulation-
dc.subject.keywordAuthorProtein-protein interaction-
dc.subject.keywordPlusMISSENSE MUTATION-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusDNA-BINDING-
dc.subject.keywordPlusGENE-
dc.subject.keywordPlusHOMEODOMAIN-
dc.subject.keywordPlusPROTEIN-
dc.subject.keywordPlusDOMAIN-
dc.subject.keywordPlusTRANSACTIVATION-
dc.subject.keywordPlusANIRIDIA-
dc.subject.keywordPlusCOMPLEX-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.description.journalRegisteredClasssci-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
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