NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80.

Journal of Biomolecular NMR
Naotaka SekiyamaMasahiro Shirakawa

Abstract

Ubiquitin is a post-translational modifier that is involved in cellular functions through its covalent attachment to target proteins. Ubiquitin can also be conjugated to itself at seven lysine residues and at its amino terminus to form eight linkage-specific polyubiquitin chains for individual cellular processes. The Lys63-linked polyubiquitin chain is recognized by tandem ubiquitin-interacting motifs (tUIMs) of Rap80 for the regulation of DNA repair. To understand the recognition mechanism between the Lys63-linked diubiquitin (K63-Ub(2)) and the tUIMs in solution, we determined the solution structure of the K63-Ub(2):tUIMs complex by using NOE restraints and RDC data derived from NMR spectroscopy. The structure showed that the tUIMs adopts a nearly straight and single continuous α-helix, and the two ubiquitin units of the K63-Ub(2) separately bind to each UIM motif. The interfaces are formed between Ile44-centered patches of the two ubiquitin units and the hydrophobic residues of the tUIMs. We also showed that the linker region between the two UIM motifs possesses a random-coil conformation in the free state, but undergoes the coil-to-helix transition upon complex formation, which simultaneously fixes the relative position of ...Continue Reading

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Citations

Jul 31, 2013·Mutation Research·Inbal Mermershtain, J N Mark Glover
Sep 11, 2013·Proceedings of the National Academy of Sciences of the United States of America·Fangtian HuangAlexander Sorkin
Feb 24, 2016·Trends in Biochemical Sciences·Caterina AlfanoAnnalisa Pastore
Oct 17, 2015·Tumour Biology : the Journal of the International Society for Oncodevelopmental Biology and Medicine·Peng Chen, Guo-Dong Yao
Jun 19, 2012·Biochemical and Biophysical Research Communications·Donghyuk ShinSangho Lee
May 26, 2012·Journal of Peptide Science : an Official Publication of the European Peptide Society·Alicja KluczykZbigniew Szewczuk
Jun 7, 2018·Science Signaling·Pengda LiuWenyi Wei

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