Zinc-Dependent Oligomerization of Thermus thermophilus Trigger Factor Chaperone

Thermus thermophilus trigger factor (TtTF) is a zinc-dependent molecular chaperone whose folding-arrest activity is regulated by Zn2+. However, little is known about the mechanism of zinc-dependent regulation of the TtTF...

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Autores principales:	Haojie Zhu, Motonori Matsusaki, Taiga Sugawara, Koichiro Ishimori, Tomohide Saio
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	trigger factor zinc-dependent chaperone <i>Thermus thermophilus</i> thermal stability secondary structure mass spectrometry Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/9387f760265d4623b412e62eef8a4b08
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spelling	oai:doaj.org-article:9387f760265d4623b412e62eef8a4b082021-11-25T16:47:03ZZinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone10.3390/biology101111062079-7737https://doaj.org/article/9387f760265d4623b412e62eef8a4b082021-10-01T00:00:00Zhttps://www.mdpi.com/2079-7737/10/11/1106https://doaj.org/toc/2079-7737<i>Thermus thermophilus</i> trigger factor (<i>Tt</i>TF) is a zinc-dependent molecular chaperone whose folding-arrest activity is regulated by Zn<sup>2+</sup>. However, little is known about the mechanism of zinc-dependent regulation of the <i>Tt</i>TF activity. Here we exploit in vitro biophysical experiments to investigate zinc-binding, the oligomeric state, the secondary structure, and the thermal stability of <i>Tt</i>TF in the absence and presence of Zn<sup>2+</sup>. The data show that full-length <i>Tt</i>TF binds Zn<sup>2+</sup>, but the isolated domains and tandem domains of <i>Tt</i>TF do not bind to Zn<sup>2+</sup>. Furthermore, circular dichroism (CD) and nuclear magnetic resonance (NMR) spectra suggested that Zn<sup>2+</sup>-binding induces the partial structural changes of <i>Tt</i>TF, and size exclusion chromatography-multi-angle light scattering (SEC-MALS) showed that Zn<sup>2+</sup> promotes <i>Tt</i>TF oligomerization. Given the previous work showing that the activity regulation of <i>E. coli</i> trigger factor is accompanied by oligomerization, the data suggest that <i>Tt</i>TF exploits zinc ions to induce the structural change coupled with the oligomerization to assemble the client-binding site, thereby effectively preventing proteins from misfolding in the thermal environment.Haojie ZhuMotonori MatsusakiTaiga SugawaraKoichiro IshimoriTomohide SaioMDPI AGarticletrigger factorzinc-dependent chaperone<i>Thermus thermophilus</i>thermal stabilitysecondary structuremass spectrometryBiology (General)QH301-705.5ENBiology, Vol 10, Iss 1106, p 1106 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	trigger factor zinc-dependent chaperone <i>Thermus thermophilus</i> thermal stability secondary structure mass spectrometry Biology (General) QH301-705.5
spellingShingle	trigger factor zinc-dependent chaperone <i>Thermus thermophilus</i> thermal stability secondary structure mass spectrometry Biology (General) QH301-705.5 Haojie Zhu Motonori Matsusaki Taiga Sugawara Koichiro Ishimori Tomohide Saio Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone
description	<i>Thermus thermophilus</i> trigger factor (<i>Tt</i>TF) is a zinc-dependent molecular chaperone whose folding-arrest activity is regulated by Zn<sup>2+</sup>. However, little is known about the mechanism of zinc-dependent regulation of the <i>Tt</i>TF activity. Here we exploit in vitro biophysical experiments to investigate zinc-binding, the oligomeric state, the secondary structure, and the thermal stability of <i>Tt</i>TF in the absence and presence of Zn<sup>2+</sup>. The data show that full-length <i>Tt</i>TF binds Zn<sup>2+</sup>, but the isolated domains and tandem domains of <i>Tt</i>TF do not bind to Zn<sup>2+</sup>. Furthermore, circular dichroism (CD) and nuclear magnetic resonance (NMR) spectra suggested that Zn<sup>2+</sup>-binding induces the partial structural changes of <i>Tt</i>TF, and size exclusion chromatography-multi-angle light scattering (SEC-MALS) showed that Zn<sup>2+</sup> promotes <i>Tt</i>TF oligomerization. Given the previous work showing that the activity regulation of <i>E. coli</i> trigger factor is accompanied by oligomerization, the data suggest that <i>Tt</i>TF exploits zinc ions to induce the structural change coupled with the oligomerization to assemble the client-binding site, thereby effectively preventing proteins from misfolding in the thermal environment.
format	article
author	Haojie Zhu Motonori Matsusaki Taiga Sugawara Koichiro Ishimori Tomohide Saio
author_facet	Haojie Zhu Motonori Matsusaki Taiga Sugawara Koichiro Ishimori Tomohide Saio
author_sort	Haojie Zhu
title	Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone
title_short	Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone
title_full	Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone
title_fullStr	Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone
title_full_unstemmed	Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone
title_sort	zinc-dependent oligomerization of <i>thermus thermophilus</i> trigger factor chaperone
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/9387f760265d4623b412e62eef8a4b08
work_keys_str_mv	AT haojiezhu zincdependentoligomerizationofithermusthermophilusitriggerfactorchaperone AT motonorimatsusaki zincdependentoligomerizationofithermusthermophilusitriggerfactorchaperone AT taigasugawara zincdependentoligomerizationofithermusthermophilusitriggerfactorchaperone AT koichiroishimori zincdependentoligomerizationofithermusthermophilusitriggerfactorchaperone AT tomohidesaio zincdependentoligomerizationofithermusthermophilusitriggerfactorchaperone
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Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone

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