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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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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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. |
format | Online Article Text |
id | pubmed-8509488 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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