DC Field | Value | Language |
---|---|---|
dc.contributor.author | In, Suna | ko |
dc.contributor.author | Kim, Yong-In | ko |
dc.contributor.author | Lee, J. Eugene | ko |
dc.contributor.author | Kim, Jaehoon | ko |
dc.date.accessioned | 2019-06-03T08:25:29Z | - |
dc.date.available | 2019-06-03T08:25:29Z | - |
dc.date.created | 2019-06-03 | - |
dc.date.created | 2019-06-03 | - |
dc.date.created | 2019-06-03 | - |
dc.date.created | 2019-06-03 | - |
dc.date.issued | 2019-04 | - |
dc.identifier.citation | NUCLEIC ACIDS RESEARCH, v.47, no.6, pp.2840 - 2855 | - |
dc.identifier.issn | 0305-1048 | - |
dc.identifier.uri | http://hdl.handle.net/10203/262415 | - |
dc.description.abstract | RNF20/40 E3 ubiquitin ligase-mediated histone H2B monoubiquitylation plays important roles in many cellular processes, including transcriptional regulation. However, the multiple defects observed in RNF20-depleted cells suggest additional ubiquitylation targets of RNF20/40 beyond histone H2B. Here, using biochemically defined assays employing purified factors and cell-based analyses, we demonstrate that RNF20/40, in conjunction with its cognate E2 ubiquitin-conjugating enzyme RAD6, monoubiquitylates lysine 381 of eEF1BL, a heat shock transcription factor. Notably, monoubiquitylation of eEF1BL increases eEF1BL accumulation and potentiates recruitment of p-TEFb to the promoter regions of heat shock-responsive genes, leading to enhanced transcription of these genes. We further demonstrate that cooperative physical interactions among eEF1BL, RNF20/40, and HSF1 synergistically promote expression of heat shock-responsive genes. In addition to identifying eEF1BL as a novel ubiquitylation target of RNF20/40 and elucidating its function, we provide a molecular mechanism for the cooperative function of distinct transcription factors in heat shock-responsive gene transcription. | - |
dc.language | English | - |
dc.publisher | OXFORD UNIV PRESS | - |
dc.title | RNF20/40-mediated eEF1BL monoubiquitylation stimulates transcription of heat shock-responsive genes | - |
dc.type | Article | - |
dc.identifier.wosid | 000467964800017 | - |
dc.identifier.scopusid | 2-s2.0-85064527886 | - |
dc.type.rims | ART | - |
dc.citation.volume | 47 | - |
dc.citation.issue | 6 | - |
dc.citation.beginningpage | 2840 | - |
dc.citation.endingpage | 2855 | - |
dc.citation.publicationname | NUCLEIC ACIDS RESEARCH | - |
dc.identifier.doi | 10.1093/nar/gkz006 | - |
dc.contributor.localauthor | Kim, Jaehoon | - |
dc.contributor.nonIdAuthor | Kim, Yong-In | - |
dc.contributor.nonIdAuthor | Lee, J. Eugene | - |
dc.description.isOpenAccess | Y | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | RNA-POLYMERASE-II | - |
dc.subject.keywordPlus | H2B UBIQUITYLATION | - |
dc.subject.keywordPlus | HISTONE H2B | - |
dc.subject.keywordPlus | P-TEFB | - |
dc.subject.keywordPlus | UBIQUITIN | - |
dc.subject.keywordPlus | ROLES | - |
dc.subject.keywordPlus | ELONGATION | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | MONOUBIQUITINATION | - |
dc.subject.keywordPlus | QUANTIFICATION | - |
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