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Chain assembly and disassembly processes differently affect the conformational space of ubiquitin chains

Item Type:Article
Title:Chain assembly and disassembly processes differently affect the conformational space of ubiquitin chains
Creators Name:Kniss, A. and Schuetz, D. and Kazemi, S. and Pluska, L. and Spindler, P.E. and Rogov, V.V. and Husnjak, K. and Dikic, I. and Güntert, P. and Sommer, T. and Prisner, T.F. and Dötsch, V.
Abstract:Ubiquitination is the most versatile posttranslational modification. The information is encoded by linkage type as well as chain length, which are translated by ubiquitin binding domains into specific signaling events. Chain topology determines the conformational space of a ubiquitin chain and adds an additional regulatory layer to this ubiquitin code. In particular, processes that modify chain length will be affected by chain conformations as they require access to the elongation or cleavage sites. We investigated conformational distributions in the context of chain elongation and disassembly using pulsed electron-electron double resonance spectroscopy in combination with molecular modeling. Analysis of the conformational space of diubiquitin revealed conformational selection or remodeling as mechanisms for chain recognition during elongation or hydrolysis, respectively. Chain elongation to tetraubiquitin increases the sampled conformational space, suggesting that a high intrinsic flexibility of K48-linked chains may contribute to efficient proteasomal degradation.
Keywords:K48-Linked Ubiquitin Chains, ERAD, PELDOR/DEER, UBDs, DUBs, Conformational Space, Structural Modeling
Source:Structure
ISSN:0969-2126
Publisher:Cell Press / Elsevier (U.S.A.)
Volume:26
Number:2
Page Range:249-258
Date:6 February 2018
Official Publication:https://doi.org/10.1016/j.str.2017.12.011
PubMed:View item in PubMed

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