Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases
DC Field | Value | Language |
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dc.contributor.author | Choi, Woo Suk | - |
dc.contributor.author | Jeong, Byung-Cheon | - |
dc.contributor.author | Joo, Yoo Jin | - |
dc.contributor.author | Lee, Myeong-Ryeol | - |
dc.contributor.author | Kim, Joon | - |
dc.contributor.author | Eck, Michael J. | - |
dc.contributor.author | Song, Hyun Kyu | - |
dc.date.accessioned | 2021-09-07T23:51:17Z | - |
dc.date.available | 2021-09-07T23:51:17Z | - |
dc.date.created | 2021-06-14 | - |
dc.date.issued | 2010-10 | - |
dc.identifier.issn | 1545-9993 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/115582 | - |
dc.description.abstract | The N-end rule pathway is a regulated proteolytic system that targets proteins containing destabilizing N-terminal residues (N-degrons) for ubiquitination and proteasomal degradation in eukaryotes. The N-degrons of type 1 substrates contain an N-terminal basic residue that is recognized by the UBR box domain of the E3 ubiquitin ligase UBR1. We describe structures of the UBR box of Saccharomyces cerevisiae UBR1 alone and in complex with N-degron peptides, including that of the cohesin subunit Scc1, which is cleaved and targeted for degradation at the metaphase-anaphase transition. The structures reveal a previously unknown protein fold that is stabilized by a novel binuclear zinc center. N-terminal arginine, lysine or histidine side chains of the N-degron are coordinated in a multispecific binding pocket. Unexpectedly, the structures together with our in vitro biochemical and in vivo pulse-chase analyses reveal a previously unknown modulation of binding specificity by the residue at position 2 of the N-degron. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.subject | ADAPTER PROTEIN CLPS | - |
dc.subject | SACCHAROMYCES-CEREVISIAE | - |
dc.subject | TERMINAL AMIDASE | - |
dc.subject | MOLECULAR-BASIS | - |
dc.subject | MICE LACKING | - |
dc.subject | PATHWAY | - |
dc.subject | DEGRADATION | - |
dc.subject | COMPONENT | - |
dc.subject | BINDING | - |
dc.subject | ARABIDOPSIS | - |
dc.title | Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Joon | - |
dc.contributor.affiliatedAuthor | Song, Hyun Kyu | - |
dc.identifier.doi | 10.1038/nsmb.1907 | - |
dc.identifier.scopusid | 2-s2.0-77957805791 | - |
dc.identifier.wosid | 000282563600005 | - |
dc.identifier.bibliographicCitation | NATURE STRUCTURAL & MOLECULAR BIOLOGY, v.17, no.10, pp.1175 - + | - |
dc.relation.isPartOf | NATURE STRUCTURAL & MOLECULAR BIOLOGY | - |
dc.citation.title | NATURE STRUCTURAL & MOLECULAR BIOLOGY | - |
dc.citation.volume | 17 | - |
dc.citation.number | 10 | - |
dc.citation.startPage | 1175 | - |
dc.citation.endPage | + | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | ADAPTER PROTEIN CLPS | - |
dc.subject.keywordPlus | SACCHAROMYCES-CEREVISIAE | - |
dc.subject.keywordPlus | TERMINAL AMIDASE | - |
dc.subject.keywordPlus | MOLECULAR-BASIS | - |
dc.subject.keywordPlus | MICE LACKING | - |
dc.subject.keywordPlus | PATHWAY | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | COMPONENT | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | ARABIDOPSIS | - |
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