| Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. | |
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MedLine Citation:
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PMID: 20835240 Owner: NLM Status: In-Process |
Abstract/OtherAbstract:
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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. |
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Authors:
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Woo Suk Choi; Byung-Cheon Jeong; Yoo Jin Joo; Myeong-Ryeol Lee; Joon Kim; Michael J Eck; Hyun Kyu Song |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-09-12 |
Journal Detail:
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Title: Nature structural & molecular biology Volume: 17 ISSN: 1545-9985 ISO Abbreviation: Nat. Struct. Mol. Biol. Publication Date: 2010 Oct |
Date Detail:
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Created Date: 2010-10-06 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101186374 Medline TA: Nat Struct Mol Biol Country: United States |
Other Details:
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Languages: eng Pagination: 1175-81 Citation Subset: IM |
Affiliation:
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School of Life Sciences and Biotechnology, Korea University, Anam-Dong, Korea. |
| Data Bank Information | |
Bank Name/Acc. No.:
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PDB/3NIH; 3NII; 3NIJ; 3NIK; 3NIL; 3NIM; 3NIN; 3NIS; 3NIT |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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| Comments/Corrections | |
Comment In:
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Nat Struct Mol Biol. 2010 Oct;17(10):1164-5
[PMID:
20924402
]
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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