Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33

Hsp33, a prokaryotic redox-regulated holding chaperone, has been recently identified to be able to exhibit an unfoldase and aggregase activity against elongation factor Tu (EF-Tu) in its reduced state. In this study, we investigated the effect of elongation factor Ts (EF-Ts) and trigger factor (TF)...

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Autores principales:	Minho Keum, Dai Ito, Mi-Seong Kim, Yuxi Lin, Kyeong-Hyeon Yoon, Jihoon Kim, Sung-Hee Lee, Ji-Hun Kim, Wookyung Yu, Young-Ho Lee, Hyung-Sik Won
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	aggregase activity EF-Tu EF-Ts proteostasis Hsp33 molecular chaperone Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/6f6a22656d4b4dc8aa63c07bce5f7872
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spelling	oai:doaj.org-article:6f6a22656d4b4dc8aa63c07bce5f78722021-11-25T16:47:40ZMolecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp3310.3390/biology101111712079-7737https://doaj.org/article/6f6a22656d4b4dc8aa63c07bce5f78722021-11-01T00:00:00Zhttps://www.mdpi.com/2079-7737/10/11/1171https://doaj.org/toc/2079-7737Hsp33, a prokaryotic redox-regulated holding chaperone, has been recently identified to be able to exhibit an unfoldase and aggregase activity against elongation factor Tu (EF-Tu) in its reduced state. In this study, we investigated the effect of elongation factor Ts (EF-Ts) and trigger factor (TF) on Hsp33-mediated EF-Tu unfolding and aggregation using gel filtration, light scattering, circular dichroism, and isothermal titration calorimetry. We found that EF-Tu unfolding and subsequent aggregation induced by Hsp33 were evident even in its complex state with EF-Ts, which enhanced EF-Tu stability. In addition, although TF alone had no substantial effect on the stability of EF-Tu, it markedly amplified the Hsp33-mediated EF-Tu unfolding and aggregation. Collectively, the present results constitute the first example of synergistic unfoldase/aggregase activity of molecular chaperones and suggest that the stability of EF-Tu is modulated by a sophisticated network of molecular chaperones to regulate protein biosynthesis in cells under stress conditions.Minho KeumDai ItoMi-Seong KimYuxi LinKyeong-Hyeon YoonJihoon KimSung-Hee LeeJi-Hun KimWookyung YuYoung-Ho LeeHyung-Sik WonMDPI AGarticleaggregase activityEF-TuEF-TsproteostasisHsp33molecular chaperoneBiology (General)QH301-705.5ENBiology, Vol 10, Iss 1171, p 1171 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	aggregase activity EF-Tu EF-Ts proteostasis Hsp33 molecular chaperone Biology (General) QH301-705.5
spellingShingle	aggregase activity EF-Tu EF-Ts proteostasis Hsp33 molecular chaperone Biology (General) QH301-705.5 Minho Keum Dai Ito Mi-Seong Kim Yuxi Lin Kyeong-Hyeon Yoon Jihoon Kim Sung-Hee Lee Ji-Hun Kim Wookyung Yu Young-Ho Lee Hyung-Sik Won Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33
description	Hsp33, a prokaryotic redox-regulated holding chaperone, has been recently identified to be able to exhibit an unfoldase and aggregase activity against elongation factor Tu (EF-Tu) in its reduced state. In this study, we investigated the effect of elongation factor Ts (EF-Ts) and trigger factor (TF) on Hsp33-mediated EF-Tu unfolding and aggregation using gel filtration, light scattering, circular dichroism, and isothermal titration calorimetry. We found that EF-Tu unfolding and subsequent aggregation induced by Hsp33 were evident even in its complex state with EF-Ts, which enhanced EF-Tu stability. In addition, although TF alone had no substantial effect on the stability of EF-Tu, it markedly amplified the Hsp33-mediated EF-Tu unfolding and aggregation. Collectively, the present results constitute the first example of synergistic unfoldase/aggregase activity of molecular chaperones and suggest that the stability of EF-Tu is modulated by a sophisticated network of molecular chaperones to regulate protein biosynthesis in cells under stress conditions.
format	article
author	Minho Keum Dai Ito Mi-Seong Kim Yuxi Lin Kyeong-Hyeon Yoon Jihoon Kim Sung-Hee Lee Ji-Hun Kim Wookyung Yu Young-Ho Lee Hyung-Sik Won
author_facet	Minho Keum Dai Ito Mi-Seong Kim Yuxi Lin Kyeong-Hyeon Yoon Jihoon Kim Sung-Hee Lee Ji-Hun Kim Wookyung Yu Young-Ho Lee Hyung-Sik Won
author_sort	Minho Keum
title	Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33
title_short	Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33
title_full	Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33
title_fullStr	Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33
title_full_unstemmed	Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33
title_sort	molecular effects of elongation factor ts and trigger factor on the unfolding and aggregation of elongation factor tu induced by the prokaryotic molecular chaperone hsp33
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/6f6a22656d4b4dc8aa63c07bce5f7872
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Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33

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