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Targeted Preparation and NMR Spectroscopic Characterization of Lys11-Linked Ubiquitin Trimers.

التفاصيل البيبلوغرافية
العنوان: Targeted Preparation and NMR Spectroscopic Characterization of Lys11-Linked Ubiquitin Trimers.
المؤلفون: Immler F; Universität Konstanz, Department of Chemistry and Graduate School of Chemical Biology (KoRS-CB), Universitätsstraße 10, 78457, Konstanz, Germany., Schneider T; Universität Konstanz, Department of Chemistry and Graduate School of Chemical Biology (KoRS-CB), Universitätsstraße 10, 78457, Konstanz, Germany., Kovermann M; Universität Konstanz, Department of Chemistry and Graduate School of Chemical Biology (KoRS-CB), Universitätsstraße 10, 78457, Konstanz, Germany.
المصدر: Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Feb 01; Vol. 25 (3), pp. e202300670. Date of Electronic Publication: 2023 Nov 30.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Wiley-VCH Verlag Country of Publication: Germany NLM ID: 100937360 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1439-7633 (Electronic) Linking ISSN: 14394227 NLM ISO Abbreviation: Chembiochem Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Weinheim, Germany : Wiley-VCH Verlag, c2000-
مواضيع طبية MeSH: Ubiquitin*/metabolism , Polyubiquitin*, Ubiquitination ; Magnetic Resonance Spectroscopy ; Nuclear Magnetic Resonance, Biomolecular
مستخلص: Ubiquitylation refers to the attachment of mono- or poly-ubiquitin molecules to a substrate protein. To shield ubiquitin chains against potential hydrolysis, a facile, click-chemistry based approach was recently established for the generation of site-specifically conjugated ubiquitin dimers relying on triazole-linkage. Here, the preparation of such ubiquitin chains was advanced by the generation of homotypic Lys11-linked ubiquitin trimers considering an isotopic labeling scheme in a moiety-wise manner. The structural and dynamical impact on the ubiquitin unit at proximal, central, or distal position that is potentially invoked by the respective other two moieties was systematically probed by heteronuclear high-resolution NMR spectroscopic approaches. As a result, conjugating a third ubiquitin moiety to the proximal or distal site of a ubiquitin dimer does not alter structural and dynamical characteristics as it has been seen for ubiquitin dimers. This observation suggests that recognition of a homotypically assembled ubiquitin chain by a potential substrate is primarily done by screening the length of a ubiquitin chain rather than relying on subtle changes in structure or dynamic properties of single ubiquitin moieties composing the chain.
(© 2023 The Authors. ChemBioChem published by Wiley-VCH GmbH.)
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معلومات مُعتمدة: SFB969 DFG; Konstanz Research School Chemical Biology
فهرسة مساهمة: Keywords: NMR spectroscopy; click-chemistry; proteins; ubiquitylation
المشرفين على المادة: 0 (Ubiquitin)
120904-94-1 (Polyubiquitin)
تواريخ الأحداث: Date Created: 20231120 Date Completed: 20240205 Latest Revision: 20240326
رمز التحديث: 20240327
DOI: 10.1002/cbic.202300670
PMID: 37983597
قاعدة البيانات: MEDLINE
الوصف
تدمد:1439-7633
DOI:10.1002/cbic.202300670