Elucidation of the mechanism of subunit exchange in αB crystallin oligomers

Abstract AlphaB crystallin (αB-crystallin) is a key protein for maintaining the long-term transparency of the eye lens. In the eye lens, αB-crystallin is a “dynamical” oligomer regulated by subunit exchange between the oligomers. To elucidate the unsettled mechanism of subunit exchange in αB-crystal...

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Autores principales:	Rintaro Inoue, Yusuke Sakamaki, Takumi Takata, Kathleen Wood, Ken Morishima, Nobuhiro Sato, Aya Okuda, Masahiro Shimizu, Reiko Urade, Noriko Fujii, Masaaki Sugiyama
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b8a425ab410945a6aa125ea5bc530606
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spelling	oai:doaj.org-article:b8a425ab410945a6aa125ea5bc5306062021-12-02T10:48:13ZElucidation of the mechanism of subunit exchange in αB crystallin oligomers10.1038/s41598-021-82250-z2045-2322https://doaj.org/article/b8a425ab410945a6aa125ea5bc5306062021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-82250-zhttps://doaj.org/toc/2045-2322Abstract AlphaB crystallin (αB-crystallin) is a key protein for maintaining the long-term transparency of the eye lens. In the eye lens, αB-crystallin is a “dynamical” oligomer regulated by subunit exchange between the oligomers. To elucidate the unsettled mechanism of subunit exchange in αB-crystallin oligomers, the study was carried out at two different protein concentrations, 28.5 mg/mL (dense sample) and 0.45 mg/mL (dilute sample), through inverse contrast matching small-angle neutron scattering. Interestingly, the exchange rate of the dense sample was the same as that of the dilute sample. From analytical ultracentrifuge measurements, the coexistence of small molecular weight components and oligomers was detected, regardless of the protein concentration. The model proposed that subunit exchange could proceed through the assistance of monomers and other small oligomers; the key mechanism is attaching/detaching monomers and other small oligomers to/from oligomers. Moreover, this model successfully reproduced the experimental results for both dense and dilute solutions. It is concluded that the monomer and other small oligomers attaching/detaching mainly regulates the subunit exchange in αB-crystallin oligomer.Rintaro InoueYusuke SakamakiTakumi TakataKathleen WoodKen MorishimaNobuhiro SatoAya OkudaMasahiro ShimizuReiko UradeNoriko FujiiMasaaki SugiyamaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Rintaro Inoue Yusuke Sakamaki Takumi Takata Kathleen Wood Ken Morishima Nobuhiro Sato Aya Okuda Masahiro Shimizu Reiko Urade Noriko Fujii Masaaki Sugiyama Elucidation of the mechanism of subunit exchange in αB crystallin oligomers
description	Abstract AlphaB crystallin (αB-crystallin) is a key protein for maintaining the long-term transparency of the eye lens. In the eye lens, αB-crystallin is a “dynamical” oligomer regulated by subunit exchange between the oligomers. To elucidate the unsettled mechanism of subunit exchange in αB-crystallin oligomers, the study was carried out at two different protein concentrations, 28.5 mg/mL (dense sample) and 0.45 mg/mL (dilute sample), through inverse contrast matching small-angle neutron scattering. Interestingly, the exchange rate of the dense sample was the same as that of the dilute sample. From analytical ultracentrifuge measurements, the coexistence of small molecular weight components and oligomers was detected, regardless of the protein concentration. The model proposed that subunit exchange could proceed through the assistance of monomers and other small oligomers; the key mechanism is attaching/detaching monomers and other small oligomers to/from oligomers. Moreover, this model successfully reproduced the experimental results for both dense and dilute solutions. It is concluded that the monomer and other small oligomers attaching/detaching mainly regulates the subunit exchange in αB-crystallin oligomer.
format	article
author	Rintaro Inoue Yusuke Sakamaki Takumi Takata Kathleen Wood Ken Morishima Nobuhiro Sato Aya Okuda Masahiro Shimizu Reiko Urade Noriko Fujii Masaaki Sugiyama
author_facet	Rintaro Inoue Yusuke Sakamaki Takumi Takata Kathleen Wood Ken Morishima Nobuhiro Sato Aya Okuda Masahiro Shimizu Reiko Urade Noriko Fujii Masaaki Sugiyama
author_sort	Rintaro Inoue
title	Elucidation of the mechanism of subunit exchange in αB crystallin oligomers
title_short	Elucidation of the mechanism of subunit exchange in αB crystallin oligomers
title_full	Elucidation of the mechanism of subunit exchange in αB crystallin oligomers
title_fullStr	Elucidation of the mechanism of subunit exchange in αB crystallin oligomers
title_full_unstemmed	Elucidation of the mechanism of subunit exchange in αB crystallin oligomers
title_sort	elucidation of the mechanism of subunit exchange in αb crystallin oligomers
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/b8a425ab410945a6aa125ea5bc530606
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Elucidation of the mechanism of subunit exchange in αB crystallin oligomers

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