DC Field | Value | Language |
---|---|---|
dc.contributor.author | KIM, JEONG MOK | - |
dc.contributor.author | Souk, Ok-Hee | - |
dc.contributor.author | HEO, JIEUN | - |
dc.contributor.author | KIM, DASOM | - |
dc.contributor.author | Jeonghun Yeom | - |
dc.contributor.author | Varshavsky, A | - |
dc.contributor.author | YOO, JOO YEON | - |
dc.contributor.author | Cheolju Lee | - |
dc.contributor.author | Shinyeong Ju | - |
dc.contributor.author | HWANG, CHEOL SANG | - |
dc.date.accessioned | 2018-12-04T01:51:44Z | - |
dc.date.available | 2018-12-04T01:51:44Z | - |
dc.date.created | 2018-11-23 | - |
dc.date.issued | 2018-11 | - |
dc.identifier.issn | 0036-8075 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/94263 | - |
dc.description.abstract | In bacteria, nascent proteins bear the pretranslationally generated N-terminal (Nt) formyl-methionine (fMet) residue. Nt-fMet of bacterial proteins is a degradation signal, termed fMet/N-degron. By contrast, proteins synthesized by cytosolic ribosomes of eukaryotes were presumed to bear unformylated Nt-Met. Here we found that the yeast formyltransferase Fmt1, although imported into mitochondria, could also produce Nt-formylated proteins in the cytosol. Nt-formylated proteins were strongly up-regulated in stationary phase or upon starvation for specific amino acids. This up-regulation strictly required the Gcn2 kinase, which phosphorylates Fmt1 and mediates its retention in the cytosol. We also found that the Nt-fMet residues of Nt-formylated proteins act as fMet/N-degrons and identified the Psh1 ubiquitin ligase as the recognition component of the eukaryotic fMet/N-end rule pathway, which destroys Nt-formylated proteins. | - |
dc.language | English | - |
dc.publisher | AMER ASSOC ADVANCEMENT SCIENCE | - |
dc.relation.isPartOf | SCIENCE | - |
dc.title | Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway | - |
dc.type | Article | - |
dc.identifier.doi | 10.1126/science.aat0174 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | SCIENCE, v.362, no.6418, pp.1019 - + | - |
dc.identifier.wosid | 000451609000035 | - |
dc.date.tcdate | 2019-02-01 | - |
dc.citation.endPage | + | - |
dc.citation.number | 6418 | - |
dc.citation.startPage | 1019 | - |
dc.citation.title | SCIENCE | - |
dc.citation.volume | 362 | - |
dc.contributor.affiliatedAuthor | KIM, JEONG MOK | - |
dc.contributor.affiliatedAuthor | Souk, Ok-Hee | - |
dc.contributor.affiliatedAuthor | HEO, JIEUN | - |
dc.contributor.affiliatedAuthor | KIM, DASOM | - |
dc.contributor.affiliatedAuthor | YOO, JOO YEON | - |
dc.contributor.affiliatedAuthor | HWANG, CHEOL SANG | - |
dc.identifier.scopusid | 2-s2.0-85056601374 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 1 | - |
dc.description.isOpenAccess | N | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | E3 UBIQUITIN LIGASE | - |
dc.subject.keywordPlus | HISTONE H3 VARIANT | - |
dc.subject.keywordPlus | TERMINAL ACETYLATION | - |
dc.subject.keywordPlus | STRUCTURAL BASIS | - |
dc.subject.keywordPlus | SACCHAROMYCES-CEREVISIAE | - |
dc.subject.keywordPlus | FLUORESCENT PROTEINS | - |
dc.subject.keywordPlus | CELLULAR-PROTEINS | - |
dc.subject.keywordPlus | TRANSFER-RNA | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
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