HSP60 possesses a GTPase activity and mediates protein folding with HSP10

The mammalian molecular chaperone, HSP60, plays an essential role in protein homeostasis through mediating protein folding and assembly. The structure and ATP-dependent function of HSP60 has been well established in recent studies. After ATP, GTP is the major cellular nucleotide. In this paper, we h...

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Autores principales: Okamoto, Tomoya, Yamamoto, Hiroshi, Kudo, Ikuru, Matsumoto, Kazuya, Odaka, Masafumi, Grave, Ewa, Itoh, Hideaki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5717063/
https://www.ncbi.nlm.nih.gov/pubmed/29208924
http://dx.doi.org/10.1038/s41598-017-17167-7
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author Okamoto, Tomoya
Yamamoto, Hiroshi
Kudo, Ikuru
Matsumoto, Kazuya
Odaka, Masafumi
Grave, Ewa
Itoh, Hideaki
author_facet Okamoto, Tomoya
Yamamoto, Hiroshi
Kudo, Ikuru
Matsumoto, Kazuya
Odaka, Masafumi
Grave, Ewa
Itoh, Hideaki
author_sort Okamoto, Tomoya
collection PubMed
description The mammalian molecular chaperone, HSP60, plays an essential role in protein homeostasis through mediating protein folding and assembly. The structure and ATP-dependent function of HSP60 has been well established in recent studies. After ATP, GTP is the major cellular nucleotide. In this paper, we have investigated the role of GTP in the activity of HSP60. It was found that HSP60 has different properties with respect to allostery, complex formation and protein folding activity depending on the nucleoside triphosphate present. The presence of GTP slightly affected the ATPase activity of HSP60 during protein folding. These results provide clues as to the functional mechanism of the HSP60-HSP10 complex.
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spelling pubmed-57170632017-12-08 HSP60 possesses a GTPase activity and mediates protein folding with HSP10 Okamoto, Tomoya Yamamoto, Hiroshi Kudo, Ikuru Matsumoto, Kazuya Odaka, Masafumi Grave, Ewa Itoh, Hideaki Sci Rep Article The mammalian molecular chaperone, HSP60, plays an essential role in protein homeostasis through mediating protein folding and assembly. The structure and ATP-dependent function of HSP60 has been well established in recent studies. After ATP, GTP is the major cellular nucleotide. In this paper, we have investigated the role of GTP in the activity of HSP60. It was found that HSP60 has different properties with respect to allostery, complex formation and protein folding activity depending on the nucleoside triphosphate present. The presence of GTP slightly affected the ATPase activity of HSP60 during protein folding. These results provide clues as to the functional mechanism of the HSP60-HSP10 complex. Nature Publishing Group UK 2017-12-05 /pmc/articles/PMC5717063/ /pubmed/29208924 http://dx.doi.org/10.1038/s41598-017-17167-7 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Okamoto, Tomoya
Yamamoto, Hiroshi
Kudo, Ikuru
Matsumoto, Kazuya
Odaka, Masafumi
Grave, Ewa
Itoh, Hideaki
HSP60 possesses a GTPase activity and mediates protein folding with HSP10
title HSP60 possesses a GTPase activity and mediates protein folding with HSP10
title_full HSP60 possesses a GTPase activity and mediates protein folding with HSP10
title_fullStr HSP60 possesses a GTPase activity and mediates protein folding with HSP10
title_full_unstemmed HSP60 possesses a GTPase activity and mediates protein folding with HSP10
title_short HSP60 possesses a GTPase activity and mediates protein folding with HSP10
title_sort hsp60 possesses a gtpase activity and mediates protein folding with hsp10
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5717063/
https://www.ncbi.nlm.nih.gov/pubmed/29208924
http://dx.doi.org/10.1038/s41598-017-17167-7
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