Hydrophobic collapse of trigger factor monomer in solution.

Trigger factor (TF) is a chaperone, found in bacterial cells and chloroplasts, that interacts with nascent polypeptide chains to suppress aggregation. While its crystal structure has been resolved, the solution structure and dynamics are largely unknown. We performed multiple molecular dynamics simu...

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Autores principales:	Kushagra Singhal, Jocelyne Vreede, Alireza Mashaghi, Sander J Tans, Peter G Bolhuis
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/499977ccd47d4c2e8e612025f5d20fe4
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spelling	oai:doaj.org-article:499977ccd47d4c2e8e612025f5d20fe42021-11-18T07:51:06ZHydrophobic collapse of trigger factor monomer in solution.1932-620310.1371/journal.pone.0059683https://doaj.org/article/499977ccd47d4c2e8e612025f5d20fe42013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23565160/?tool=EBIhttps://doaj.org/toc/1932-6203Trigger factor (TF) is a chaperone, found in bacterial cells and chloroplasts, that interacts with nascent polypeptide chains to suppress aggregation. While its crystal structure has been resolved, the solution structure and dynamics are largely unknown. We performed multiple molecular dynamics simulations on Trigger factor in solution, and show that its tertiary domains display collective motions hinged about inter-domain linkers with minimal or no loss in secondary structure. Moreover, we find that isolated TF typically adopts a collapsed state, with the formation of domain pairs. This collapse of TF in solution is induced by hydrophobic interactions and stabilised by hydrophilic contacts. To determine the nature of the domain interactions, we analysed the hydrophobicity of the domain surfaces by using the hydrophobic probe method of Acharya et al., as the standard hydrophobicity scales predictions are limited due to the complex environment. We find that the formation of domain pairs changes the hydrophobic map of TF, making the N-terminal and arm2 domain pair more hydrophilic and the head and arm1 domain pair more hydrophobic. These insights into the dynamics and interactions of the TF domains are important to eventually understand chaperone-substrate interactions and chaperone function.Kushagra SinghalJocelyne VreedeAlireza MashaghiSander J TansPeter G BolhuisPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 4, p e59683 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kushagra Singhal Jocelyne Vreede Alireza Mashaghi Sander J Tans Peter G Bolhuis Hydrophobic collapse of trigger factor monomer in solution.
description	Trigger factor (TF) is a chaperone, found in bacterial cells and chloroplasts, that interacts with nascent polypeptide chains to suppress aggregation. While its crystal structure has been resolved, the solution structure and dynamics are largely unknown. We performed multiple molecular dynamics simulations on Trigger factor in solution, and show that its tertiary domains display collective motions hinged about inter-domain linkers with minimal or no loss in secondary structure. Moreover, we find that isolated TF typically adopts a collapsed state, with the formation of domain pairs. This collapse of TF in solution is induced by hydrophobic interactions and stabilised by hydrophilic contacts. To determine the nature of the domain interactions, we analysed the hydrophobicity of the domain surfaces by using the hydrophobic probe method of Acharya et al., as the standard hydrophobicity scales predictions are limited due to the complex environment. We find that the formation of domain pairs changes the hydrophobic map of TF, making the N-terminal and arm2 domain pair more hydrophilic and the head and arm1 domain pair more hydrophobic. These insights into the dynamics and interactions of the TF domains are important to eventually understand chaperone-substrate interactions and chaperone function.
format	article
author	Kushagra Singhal Jocelyne Vreede Alireza Mashaghi Sander J Tans Peter G Bolhuis
author_facet	Kushagra Singhal Jocelyne Vreede Alireza Mashaghi Sander J Tans Peter G Bolhuis
author_sort	Kushagra Singhal
title	Hydrophobic collapse of trigger factor monomer in solution.
title_short	Hydrophobic collapse of trigger factor monomer in solution.
title_full	Hydrophobic collapse of trigger factor monomer in solution.
title_fullStr	Hydrophobic collapse of trigger factor monomer in solution.
title_full_unstemmed	Hydrophobic collapse of trigger factor monomer in solution.
title_sort	hydrophobic collapse of trigger factor monomer in solution.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/499977ccd47d4c2e8e612025f5d20fe4
work_keys_str_mv	AT kushagrasinghal hydrophobiccollapseoftriggerfactormonomerinsolution AT jocelynevreede hydrophobiccollapseoftriggerfactormonomerinsolution AT alirezamashaghi hydrophobiccollapseoftriggerfactormonomerinsolution AT sanderjtans hydrophobiccollapseoftriggerfactormonomerinsolution AT petergbolhuis hydrophobiccollapseoftriggerfactormonomerinsolution
_version_	1718422847605440512

Hydrophobic collapse of trigger factor monomer in solution.

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