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Title: Ubiquitylation Directly Induces Fold Destabilization of Proteins
Authors: Morimoto, Daichi  kyouindb  KAKEN_id  orcid (unconfirmed)
Walinda, Erik  kyouindb  KAKEN_id  orcid (unconfirmed)
Fukada, Harumi
Sugase, Kenji  kyouindb  KAKEN_id  orcid (unconfirmed)
Shirakawa, Masahiro
Author's alias: 森本, 大智
菅瀬, 謙治
白川, 昌宏
Issue Date: 19-Dec-2016
Publisher: Springer Nature
Journal title: Scientific Reports
Volume: 6
Thesis number: 39453
Abstract: Ubiquitin is a common post-Translational modifier and its conjugation is a key signal for proteolysis by the proteasome. Because the molecular mass of ubiquitin is larger than that of other modifiers such as phosphate, acetyl, or methyl groups, ubiquitylation not only influences biochemical signaling, but also may exert physical effects on its substrate proteins by increasing molecular volume and altering shape anisotropy. Here we show that ubiquitylation destabilizes the fold of two proteins, FKBP12 and FABP4, and that elongation of the conjugated ubiquitin chains further enhances this destabilization effect. Moreover, NMR relaxation analysis shows that ubiquitylation induces characteristic structural fluctuations in the backbone of both proteins. These results suggest that the ubiquitylation-driven structural fluctuations lead to fold destabilization of its substrate proteins. Thus, physical destabilization by ubiquitylation may facilitate protein degradation by the proteasome.
Rights: © The Author(s) 2016. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit
DOI(Published Version): 10.1038/srep39453
PubMed ID: 27991582
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