DC Field | Value | Language |
---|---|---|
dc.contributor.author | Hyun, Kwang Beom | ko |
dc.contributor.author | Xu, Xiaonan | ko |
dc.contributor.author | Li, Haitao | ko |
dc.contributor.author | Kim, Jaehoon | ko |
dc.date.accessioned | 2017-07-18T06:26:46Z | - |
dc.date.available | 2017-07-18T06:26:46Z | - |
dc.date.created | 2017-07-13 | - |
dc.date.issued | 2017-06-27 | - |
dc.identifier.citation | 2017 Epigenetic Regulatory Pathways | - |
dc.identifier.uri | http://hdl.handle.net/10203/224835 | - |
dc.description.abstract | In yeast, H3K4 methylation, the hallmark of active transcription, is known to be dependent on H2B ubiquitylation. We want to understand the mechanism of H2B mono-ubiquitylation by E3 ubiquitin ligase Bre1and E2 ubiquitin conjugating enzyme Rad6. Bre1 has a coiled coil motif (CCM) at the N-terminus and a RING finger domain at the C-terminal end. Previous studies have well confirmed the Interaction between Bre1-CCM and Rad6. This interaction is non-canonical E2-E3 interaction because most of the E2 enzyme binds to the RING-finger domain of E3. By co-expressing Bre1-CCM and Rad6 in E.coli, we purified the Bre1-CCM/Rad6 complex and further identified the X-ray crystal structure. To validate the structure obtained from X-ray crystallography, we further purified various mutant proteins and observed the interaction change between two proteins and also H2B ubiquitylation activity. | - |
dc.language | English | - |
dc.publisher | Abcam | - |
dc.title | Molecular mechanism of Bre1-Rad6 mediated H2B ubiquitylation | - |
dc.type | Conference | - |
dc.type.rims | CONF | - |
dc.citation.publicationname | 2017 Epigenetic Regulatory Pathways | - |
dc.identifier.conferencecountry | KO | - |
dc.identifier.conferencelocation | Millennium Seoul Hilton, Seoul | - |
dc.contributor.localauthor | Kim, Jaehoon | - |
dc.contributor.nonIdAuthor | Xu, Xiaonan | - |
dc.contributor.nonIdAuthor | Li, Haitao | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.