Structural and Dynamic Characterization of Artificially Linked Ubiquitin Dimers by NMR spectroscopy.
Related Articles Structural and Dynamic Characterization of Artificially Linked Ubiquitin Dimers by NMR spectroscopy.
Chembiochem. 2019 Mar 28;:
Authors: Zhao X, Mißun M, Schneider T, Müller F, Lutz J, Scheffner M, Marx A, Kovermann M
Abstract
As one of the most prevalent post-translational modifications in eukaryotic cells, ubiquitylation plays vital roles in many cellular processes such as protein degradation, DNA metabolism, and cell differentiation. Substrate proteins can be tagged by distinct types of polymeric ubiquitin (Ub) chains, which determine the eventual fate of the modified protein. We recently established a facile, click chemistry-based approach for the efficient generation of linkage-defined Ub chains including Ub dimers. Within these chains, individual Ub moieties are connected via a triazole linkage rather than the natural isopeptide bond. Here, we report that the conformation of an artificially K48-linked Ub dimer resembles that of the natively linked dimer with respect to structural and dynamic characteristics, as demonstrated by high-resolution NMR spectroscopy. Thus, we conclude that artificially linked Ub dimers, as generated by our approach, represent potent tools for studying the inherently different properties and functions of distinct Ub chains.
PMID: 30920720 [PubMed - as supplied by publisher]
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