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Title: New insight into the dynamical system of αB-crystallin oligomers
Authors: Inoue, Rintaro  kyouindb  KAKEN_id
Takata, Takumi  kyouindb  KAKEN_id
Fujii, Norihiko
Ishii, Kentaro
Uchiyama, Susumu
Sato, Nobuhiro  kyouindb  KAKEN_id  orcid (unconfirmed)
Oba, Yojiro  kyouindb  KAKEN_id
Wood, Kathleen
Kato, Koichi
Fujii, Noriko
Sugiyama, Masaaki
Author's alias: 井上, 倫太郎
髙田, 匠
佐藤, 信浩
大場, 洋次郎
藤井, 紀子
杉山, 正明
Keywords: Chaperones
Issue Date: 6-Jul-2016
Publisher: Springer Nature
Journal title: Scientific Reports
Volume: 6
Thesis number: 29208
Abstract: α-Crystallin possesses a dynamic quaternary structure mediated by its subunit dynamics. Elucidation of a mechanism of subunit dynamics in homo-oligomers of αB-crystallin was tackled through deuteration-assisted small-angle neutron scattering (DA-SANS) and electrospray ionization (ESI) native mass spectrometry (nMS). The existence of subunit exchange was confirmed with DA-SANS, and monomers liberated from the oligomers were observed with nMS. With increasing temperature, an increase in both the exchange rate and monomer population was observed despite the absence of oligomer collapse. It is proposed that transiently liberated subunits, namely, “traveling subunits, ” play a role in subunit exchange. Moreover, we propose that protein function is regulated by these traveling subunits.
Rights: 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.
DOI(Published Version): 10.1038/srep29208
PubMed ID: 27381175
Appears in Collections:Journal Articles

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