Structural basis of client specificity in mitochondrial membrane-protein chaperones-Reference-Cited by-同舟云学术

Structural basis of client specificity in mitochondrial membrane-protein chaperones

Published:2020-12-18 Issue:51 Volume:6 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Sučec Iva¹^ORCID,Wang Yong²^ORCID,Dakhlaoui Ons¹^ORCID,Weinhäupl Katharina¹^ORCID,Jores Tobias³^ORCID,Costa Doriane¹,Hessel Audrey¹,Brennich Martha⁴^ORCID,Rapaport Doron³^ORCID,Lindorff-Larsen Kresten²^ORCID,Bersch Beate¹^ORCID,Schanda Paul¹^ORCID

Affiliation:

1. Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, Avenue des Martyrs, F-38044 Grenoble, France.

2. Structural Biology and NMR Laboratory, the Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark.

3. Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany.

4. European Molecular Biology Laboratory, 38042 Grenoble, France.

Abstract

A balance of dynamic hydrophobic and hydrophilic contacts enables client specificity in mitochondrial membrane-protein chaperones.

Funder

FP7 Ideas: European Research Council

Deutsche Forschungsgemeinschaft

Agence Nationale de la Recherche

Lundbeckfonden

Novo Nordisk Fonden

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference61 articles.

1. Biological and Chemical Approaches to Diseases of Proteostasis Deficiency

2. Molecular Chaperone Functions in Protein Folding and Proteostasis

3. Cytosolic targeting factor AKR2A captures chloroplast outer membrane-localized client proteins at the ribosome during translation

4. Substrate specificity in the context of molecular chaperones

5. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

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