BROWSE

Related Scientist

kim,yunju's photo.

kim,yunju
유전체교정연구단
more info

ITEM VIEW & DOWNLOAD

POWERDRESS and HDA9 interact and promote histone H3 deacetylation at specific genomic sites in Arabidopsis

DC Field Value Language
dc.contributor.authorYun Ju Kim-
dc.contributor.authorWang, Ruozhong-
dc.contributor.authorGao, Lei-
dc.contributor.authorLi Dongming-
dc.contributor.authorXu, Chi-
dc.contributor.authorHyunggon Mang-
dc.contributor.authorJien Jeon-
dc.contributor.authorChen, Xiangsong-
dc.contributor.authorZhong Xuehua-
dc.contributor.authorJune M. Kwak-
dc.contributor.authorMo, Beixin-
dc.contributor.authorXiao Langtao-
dc.contributor.authorChen, Xuemei-
dc.date.available2017-01-05T01:50:06Z-
dc.date.created2017-01-03-
dc.date.issued2016-12-
dc.identifier.issn0027-8424-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/3156-
dc.description.abstractHistone acetylation is a major epigenetic control mechanism that is tightly linked to the promotion of gene expression. Histone acetylation levels are balanced through the opposing activities of histone acetyltransferases (HATs) and histone deacetylases (HDACs). Arabidopsis HDAC genes (AtHDACs) compose a large gene family, and distinct phenotypes among AtHDAC mutants reflect the functional specificity of individual AtHDACs. However, the mechanisms underlying this functional diversity are largely unknown. Here, we show that POWERDRESS (PWR), a SANT (SWI3/DAD2/N-CoR/TFIII-B) domain protein, interacts with HDA9 and promotes histone H3 deacetylation, possibly by facilitating HDA9 function at target regions. The developmental phenotypes of pwr and hda9 mutants were highly similar. Three lysine residues (K9, K14, and K27) of H3 retained hyperacetylation status in both pwr and hda9 mutants. Genome-wide H3K9 and H3K14 acetylation profiling revealed elevated acetylation at largely overlapping sets of target genes in the two mutants. Highly similar gene-expression profiles in the twomutants correlated with the histone H3 acetylation status in the pwr and hda9 mutants. In addition, PWR and HDA9 modulated flowering time by repressing AGAMOUS-LIKE 19 expression through histone H3 deacetylation in the same genetic pathway. Finally, PWR was shown to physically interact with HDA9, and its SANT2 domain, which is homologous to that of subunits in animal HDAC complexes, showed specific binding affinity to acetylated histone H3.We therefore propose that PWR acts as a subunit in a complex with HDA9 to result in lysine deacetylation of histone H3 at specific genomic targets.-
dc.description.uri1-
dc.language영어-
dc.publisherNATL ACAD SCIENCES-
dc.subjectSANT domain | POWERDRESS | HDA9 | histone deacetylation | AGL19-
dc.titlePOWERDRESS and HDA9 interact and promote histone H3 deacetylation at specific genomic sites in Arabidopsis-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000390044900083-
dc.identifier.scopusid2-s2.0-85006371881-
dc.identifier.rimsid58124ko
dc.date.tcdate2018-10-01-
dc.contributor.affiliatedAuthorYun Ju Kim-
dc.contributor.affiliatedAuthorHyunggon Mang-
dc.contributor.affiliatedAuthorJien Jeon-
dc.contributor.affiliatedAuthorJune M. Kwak-
dc.identifier.doi10.1073/pnas.1618618114-
dc.identifier.bibliographicCitationPROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.113, no.51, pp.14858 - 14863-
dc.citation.titlePROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-
dc.citation.volume113-
dc.citation.number51-
dc.citation.startPage14858-
dc.citation.endPage14863-
dc.date.scptcdate2018-10-01-
dc.description.wostc6-
dc.description.scptc7-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.subject.keywordPlusSANT DOMAIN-
dc.subject.keywordPlusN-COR-
dc.subject.keywordPlusFLOWERING TIME-
dc.subject.keywordPlusACETYLATION-
dc.subject.keywordPlusREPRESSION-
dc.subject.keywordPlusGENES-
dc.subject.keywordPlusIDENTIFICATION-
dc.subject.keywordPlusTRANSCRIPTION-
dc.subject.keywordPlusTHALIANA-
dc.subject.keywordPlusTOPLESS-
dc.subject.keywordAuthorSANT domain-
dc.subject.keywordAuthorPOWERDRESS-
dc.subject.keywordAuthorHDA9-
dc.subject.keywordAuthorhistone deacetylation-
dc.subject.keywordAuthorAGL19-
Appears in Collections:
Center for Plant Aging Research (식물 노화·수명 연구단) > 1. Journal Papers (저널논문)
Files in This Item:
김윤주박사님 논문.pdfDownload

qrcode

  • facebook

    twitter

  • Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse