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Oligomeric Structural Transition of HspB1 from Chinese Hamster

HspB1 is a mammalian sHsp that is ubiquitously expressed in almost all tissues and involved in regulating many vital functions. Although the recent crystal structure of human HspB1 showed that 24 monomers form the oligomeric complex of human HspB1 in a spherical configuration, the molecular architec...

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Autores principales: Kurokawa, Nina, Midorikawa, Rio, Nakamura, Manami, Noguchi, Keiichi, Morishima, Ken, Inoue, Rintaro, Sugiyama, Masaaki, Yohda, Masafumi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8509488/
https://www.ncbi.nlm.nih.gov/pubmed/34639138
http://dx.doi.org/10.3390/ijms221910797
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author Kurokawa, Nina
Midorikawa, Rio
Nakamura, Manami
Noguchi, Keiichi
Morishima, Ken
Inoue, Rintaro
Sugiyama, Masaaki
Yohda, Masafumi
author_facet Kurokawa, Nina
Midorikawa, Rio
Nakamura, Manami
Noguchi, Keiichi
Morishima, Ken
Inoue, Rintaro
Sugiyama, Masaaki
Yohda, Masafumi
author_sort Kurokawa, Nina
collection PubMed
description HspB1 is a mammalian sHsp that is ubiquitously expressed in almost all tissues and involved in regulating many vital functions. Although the recent crystal structure of human HspB1 showed that 24 monomers form the oligomeric complex of human HspB1 in a spherical configuration, the molecular architecture of HspB1 is still controversial. In this study, we examined the oligomeric structural change of CgHspB1 by sedimentation velocity analytical ultracentrifugation. At the low temperature of 4 °C, CgHspB1 exists as an 18-mer, probably a trimeric complex of hexamers. It is relatively unstable and partially dissociates into small oligomers, hexamers, and dodecamers. At elevated temperatures, the 24-mer was more stable than the 18-mer. The 24-mer is also in dynamic equilibrium with the dissociated oligomers in the hexameric unit. The hexamer further dissociates to dimers. The disulfide bond between conserved cysteine residues seems to be partly responsible for the stabilization of hexamers. The N-terminal domain is involved in the assembly of dimers and the interaction between hexamers. It is plausible that CgHspB1 expresses a chaperone function in the 24-mer structure.
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spelling pubmed-85094882021-10-13 Oligomeric Structural Transition of HspB1 from Chinese Hamster Kurokawa, Nina Midorikawa, Rio Nakamura, Manami Noguchi, Keiichi Morishima, Ken Inoue, Rintaro Sugiyama, Masaaki Yohda, Masafumi Int J Mol Sci Article HspB1 is a mammalian sHsp that is ubiquitously expressed in almost all tissues and involved in regulating many vital functions. Although the recent crystal structure of human HspB1 showed that 24 monomers form the oligomeric complex of human HspB1 in a spherical configuration, the molecular architecture of HspB1 is still controversial. In this study, we examined the oligomeric structural change of CgHspB1 by sedimentation velocity analytical ultracentrifugation. At the low temperature of 4 °C, CgHspB1 exists as an 18-mer, probably a trimeric complex of hexamers. It is relatively unstable and partially dissociates into small oligomers, hexamers, and dodecamers. At elevated temperatures, the 24-mer was more stable than the 18-mer. The 24-mer is also in dynamic equilibrium with the dissociated oligomers in the hexameric unit. The hexamer further dissociates to dimers. The disulfide bond between conserved cysteine residues seems to be partly responsible for the stabilization of hexamers. The N-terminal domain is involved in the assembly of dimers and the interaction between hexamers. It is plausible that CgHspB1 expresses a chaperone function in the 24-mer structure. MDPI 2021-10-06 /pmc/articles/PMC8509488/ /pubmed/34639138 http://dx.doi.org/10.3390/ijms221910797 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Kurokawa, Nina
Midorikawa, Rio
Nakamura, Manami
Noguchi, Keiichi
Morishima, Ken
Inoue, Rintaro
Sugiyama, Masaaki
Yohda, Masafumi
Oligomeric Structural Transition of HspB1 from Chinese Hamster
title Oligomeric Structural Transition of HspB1 from Chinese Hamster
title_full Oligomeric Structural Transition of HspB1 from Chinese Hamster
title_fullStr Oligomeric Structural Transition of HspB1 from Chinese Hamster
title_full_unstemmed Oligomeric Structural Transition of HspB1 from Chinese Hamster
title_short Oligomeric Structural Transition of HspB1 from Chinese Hamster
title_sort oligomeric structural transition of hspb1 from chinese hamster
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8509488/
https://www.ncbi.nlm.nih.gov/pubmed/34639138
http://dx.doi.org/10.3390/ijms221910797
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