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Title: Hydrogen-deuterium exchange profiles of polyubiquitin fibrils
Authors: Morimoto, Daichi  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-7672-2136 (unconfirmed)
Nishizawa, Ryo
Walinda, Erik
Takashima, Shingo
Sugase, Kenji  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0001-8623-7743 (unconfirmed)
Shirakawa, Masahiro
Author's alias: 森本, 大智
菅瀬, 謙治
白川, 昌宏
Keywords: Amyloid fibrils
Hydrogen-deuterium exchange
Ubiquitin
Issue Date: Mar-2018
Publisher: MDPI AG
Journal title: Polymers
Volume: 10
Issue: 3
Thesis number: 240
Abstract: Ubiquitin and its polymeric forms are conjugated to intracellular proteins to regulate diverse intracellular processes. Intriguingly, polyubiquitin has also been identified as a component of pathological protein aggregates associated with Alzheimer’s disease and other neurodegenerative disorders. We recently found that polyubiquitin can form amyloid-like fibrils, and that these fibrillar aggregates can be degraded by macroautophagy. Although the structural properties appear to function in recognition of the fibrils, no structural information on polyubiquitin fibrils has been reported so far. Here, we identify the core of M1-linked diubiquitin fibrils from hydrogen-deuterium exchange experiments using solution nuclear magnetic resonance (NMR) spectroscopy. Intriguingly, intrinsically flexible regions became highly solvent-protected in the fibril structure. These results indicate that polyubiquitin fibrils are formed by inter-molecular interactions between relatively flexible structural components, including the loops and edges of secondary structure elements.
Rights: © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
URI: http://hdl.handle.net/2433/233917
DOI(Published Version): 10.3390/polym10030240
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