Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 김정목 | - |
dc.date.accessioned | 2019-12-10T02:12:30Z | - |
dc.date.available | 2019-12-10T02:12:30Z | - |
dc.date.issued | 2018-11 | - |
dc.identifier.citation | SCIENCE, v. 362, no. 6418, page. 1019-+, Article no. eaat0174 | en_US |
dc.identifier.issn | 0036-8075 | - |
dc.identifier.issn | 1095-9203 | - |
dc.identifier.uri | https://science.sciencemag.org/content/362/6418/eaat0174 | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/120629 | - |
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. | en_US |
dc.description.sponsorship | This work was supported by grants from the Samsung Science & Technology Foundation (SSTF-BA1401-17) and the BK21 plus program (C.-S. H.), by NRF grants of the Korean Government (MSIP) [NRF-2017M3A9F9030559 (C. L.) and NRF-2017R1A5A1015366 (J.-Y.Y.)], and by NIH grants R01GM031530 and R01DK039520 (A.V.). | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | AMER ASSOC ADVANCEMENT SCIENCE | en_US |
dc.subject | E3 UBIQUITIN LIGASE | en_US |
dc.subject | HISTONE H3 VARIANT | en_US |
dc.subject | TERMINAL ACETYLATION | en_US |
dc.subject | STRUCTURAL BASIS | en_US |
dc.subject | SACCHAROMYCES-CEREVISIAE | en_US |
dc.subject | FLUORESCENT PROTEINS | en_US |
dc.subject | CELLULAR-PROTEINS | en_US |
dc.subject | TRANSFER-RNA | en_US |
dc.subject | DEGRADATION | en_US |
dc.subject | RECOGNITION | en_US |
dc.title | Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway | en_US |
dc.type | Article | en_US |
dc.relation.no | 6418 | - |
dc.relation.volume | 362 | - |
dc.identifier.doi | 10.1126/science.aat0174 | - |
dc.relation.page | 1019-1019 | - |
dc.relation.journal | SCIENCE | - |
dc.contributor.googleauthor | Kim, Jeong-Mok | - |
dc.contributor.googleauthor | Seok, Ok-Hee | - |
dc.contributor.googleauthor | Ju, Shinyeong | - |
dc.contributor.googleauthor | Heo, Ji-Eun | - |
dc.contributor.googleauthor | Yeom, Jeonghun | - |
dc.contributor.googleauthor | Kim, Da-Som | - |
dc.contributor.googleauthor | Yoo, Joo-Yeon | - |
dc.contributor.googleauthor | Varshavsky, Alexander | - |
dc.contributor.googleauthor | Lee, Cheolju | - |
dc.contributor.googleauthor | Hwang, Cheol-Sang | - |
dc.relation.code | 2018001772 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF NATURAL SCIENCES[S] | - |
dc.sector.department | DEPARTMENT OF LIFE SCIENCE | - |
dc.identifier.pid | jmokkim | - |
dc.identifier.orcid | http://orcid.org/0000-0002-7223-248X | - |
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