| Mechanism-Based Small Molecule Cross-Linkers of HECT E3 Ubiquitin Ligase - Substrate Pairs. | |
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MedLine Citation:
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PMID: 23043241 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Here we report the discovery that bifunctional thiol- and amine-reactive electrophiles serve as mechanism-based covalent cross-linkers for HECT E3 ubiquitin ligase/substrate pairs. We demonstrate that these chemical cross-linkers covalently cross-link the catalytic Cys residue of the yeast HECT E3 ubiquitin ligase Rsp5 with the Lys of the ubiquitination site in the model substrate Sic60-GFP. This work represents the first example of mechanism-based covalent cross-link of HECT E3/substrate pairs that converts transiently interacting HECT E3/substrate pairs into stable, covalently cross-linked protein complexes, thereby facilitating their subsequent isolation, identification, and study. |
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Authors:
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Sungjin Park; Ioanna Ntai; Paul Martin Thomas; Evgeniia V Konishcheva; Neil L Kelleher; Alexander V Statsuk |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-10-8 |
Journal Detail:
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Title: Biochemistry Volume: - ISSN: 1520-4995 ISO Abbreviation: Biochemistry Publication Date: 2012 Oct |
Date Detail:
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Created Date: 2012-10-9 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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