DC Field | Value | Language |
---|---|---|
dc.contributor.author | Yang, Aerin | ko |
dc.contributor.author | Ha, Sura | ko |
dc.contributor.author | Ahn, Jihye | ko |
dc.contributor.author | Kim, Rira | ko |
dc.contributor.author | Kim, Sungyoon | ko |
dc.contributor.author | Lee, Younghoon | ko |
dc.contributor.author | Kim, Jaehoon | ko |
dc.contributor.author | Soell, Dieter | ko |
dc.contributor.author | Lee, Hee-Yoon | ko |
dc.contributor.author | Park, Hee-Sung | ko |
dc.date.accessioned | 2016-12-01T08:00:39Z | - |
dc.date.available | 2016-12-01T08:00:39Z | - |
dc.date.created | 2016-11-28 | - |
dc.date.created | 2016-11-28 | - |
dc.date.created | 2016-11-28 | - |
dc.date.issued | 2016-11 | - |
dc.identifier.citation | SCIENCE, v.354, no.6312, pp.623 - 626 | - |
dc.identifier.issn | 0036-8075 | - |
dc.identifier.uri | http://hdl.handle.net/10203/214602 | - |
dc.description.abstract | Many essential biological processes are controlled by posttranslational protein modifications. The inability to synthetically attain the diversity enabled by these modifications limits functional studies of many proteins. We designed a three-step approach for installing authentic posttranslational modifications in recombinant proteins. We first use the established O-phosphoserine (Sep) orthogonal translation system to create a Sep-containing recombinant protein. The Sep residue is then dephosphorylated to dehydroalanine (Dha). Last, conjugate addition of alkyl iodides to Dha, promoted by zinc and copper, enables chemoselective carbon-carbon bond formation. To validate our approach, we produced histone H3, ubiquitin, and green fluorescent protein variants with site-specific modifications, including different methylations of H3K79. The methylated histones stimulate transcription through histone acetylation. This approach offers a powerful tool to engineer diverse designer proteins | - |
dc.language | English | - |
dc.publisher | AMER ASSOC ADVANCEMENT SCIENCE | - |
dc.title | A chemical biology route to site-specific authentic protein modifications | - |
dc.type | Article | - |
dc.identifier.wosid | 000386869800050 | - |
dc.identifier.scopusid | 2-s2.0-84990855446 | - |
dc.type.rims | ART | - |
dc.citation.volume | 354 | - |
dc.citation.issue | 6312 | - |
dc.citation.beginningpage | 623 | - |
dc.citation.endingpage | 626 | - |
dc.citation.publicationname | SCIENCE | - |
dc.identifier.doi | 10.1126/science.aah4428 | - |
dc.contributor.localauthor | Lee, Younghoon | - |
dc.contributor.localauthor | Kim, Jaehoon | - |
dc.contributor.localauthor | Lee, Hee-Yoon | - |
dc.contributor.localauthor | Park, Hee-Sung | - |
dc.contributor.nonIdAuthor | Soell, Dieter | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | POSTTRANSLATIONAL MODIFICATIONS | - |
dc.subject.keywordPlus | RECOMBINANT HISTONES | - |
dc.subject.keywordPlus | LYSINE ANALOGS | - |
dc.subject.keywordPlus | BOND FORMATION | - |
dc.subject.keywordPlus | METHYL-LYSINE | - |
dc.subject.keywordPlus | GENETIC-CODE | - |
dc.subject.keywordPlus | PHOSPHOSERINE | - |
dc.subject.keywordPlus | CHEMISTRY | - |
dc.subject.keywordPlus | CYSTEINE | - |
dc.subject.keywordPlus | PEPTIDE | - |
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