DC Field | Value | Language |
---|---|---|
dc.contributor.author | 김재훈 | - |
dc.date.accessioned | 2016-07-13T07:26:58Z | - |
dc.date.available | 2016-07-13T07:26:58Z | - |
dc.date.created | 2015-12-29 | - |
dc.date.issued | 2012-12-20 | - |
dc.identifier.citation | 한국분자세포생물학회 에피유전체학분과 심포지엄 | - |
dc.identifier.uri | http://hdl.handle.net/10203/211553 | - |
dc.description.abstract | Genetic and cell-based studies have documented a cross-talk between H2B ubiquitylation (H2Bub) and H3K4 methylation, but little, if any, direct biochemical evidence exists explaining the mechanism underlying H2Bub-dependent H3K4 methylation on chromatin templates. To gain valuable insights, we have turned to an in vitro histone methyltransferase assay employing a reconstituted/purified yeast Set1 complex (ySet1C) and a recombinant chromatin template containing fully ubiquitylated H2B. In conjunction with genetic analyses, we demonstrate that the n-SET domain within Set1, but not Swd2, is essential for H2Bub-dependent H3K4 methylation. Spp1, a homolog of human CFP1, is conditionally involved in this cross-talk, and our findings extend to the human Set1 complex, underscoring the highly conserved nature of this disease-relevant, cross-talk pathway. As not all members of the known H3K4 methyltransferase family contain n-SET domains, our studies call attention to the n-SET domain as being a predictor of H2B ubiquitylation ‘sensing’ in bringing about downstream H3K4 methylation | - |
dc.language | Korean | - |
dc.publisher | 한국분자세포생물학회 에피유전체학분과 | - |
dc.title | Mechanism of H2B ubiquitylation-dependent H3K4 methylation | - |
dc.type | Conference | - |
dc.type.rims | CONF | - |
dc.citation.publicationname | 한국분자세포생물학회 에피유전체학분과 심포지엄 | - |
dc.identifier.conferencecountry | KO | - |
dc.identifier.conferencelocation | 강원도 평창 알펜시아 | - |
dc.contributor.localauthor | 김재훈 | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.