Web of Science: 9 cites, Scopus: 9 cites, Google Scholar: cites,
Disulfide driven folding for a conditionally disordered protein
Fraga, Hugo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Pujols, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Gil-Garcia, Marcos (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Roque Córdova, Alicia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Bernardo-Seisdedos, Ganeko (CIC BioGUNE)
Santambrogio, Carlo (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze)
Bech-Serra, Joan-Josep (Vall d'Hebron Institut d'Oncologia)
Canals, Francesc (Vall d'Hebron Institut d'Oncologia)
Bernadó, Pau (Centre de biochimie Structurale (Montpellier))
Grandori, Rita (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze)
Millet, Oscar (CIC BioGUNE)
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)

Data: 2017
Resum: Conditionally disordered proteins are either ordered or disordered depending on the environmental context. The substrates of the mitochondrial intermembrane space (IMS) oxidoreductase Mia40 are synthesized on cytosolic ribosomes and diffuse as intrinsically disordered proteins to the IMS, where they fold into their functional conformations; behaving thus as conditionally disordered proteins. It is not clear how the sequences of these polypeptides encode at the same time for their ability to adopt a folded structure and to remain unfolded. Here we characterize the disorder-to-order transition of a Mia40 substrate, the human small copper chaperone Cox17. Using an integrated real-time approach, including chromatography, fluorescence, CD, FTIR, SAXS, NMR, and MS analysis, we demonstrate that in this mitochondrial protein, the conformational switch between disordered and folded states is controlled by the formation of a single disulfide bond, both in the presence and in the absence of Mia40. We provide molecular details on how the folding of a conditionally disordered protein is tightly regulated in time and space, in such a way that the same sequence is competent for protein translocation and activity.
Nota: Altres ajuts: ICREA, ICREA-Academia 2015 to S.V.
Nota: Número d'acord de subvenció MINECO/BIO2016-783-78310-R
Drets: This is an open access article distributed under the terms of the , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Creative Commons
Llengua: Anglès
Document: article ; recerca ; publishedVersion
Matèria: Amino Acid Sequence ; Carrier Proteins ; Disulfides ; Humans ; Intrinsically Disordered Proteins ; Mitochondrial Membrane Transport Proteins ; Models, Molecular ; Protein Conformation ; Protein Folding ; Scattering, Small Angle ; Sequence Homology ; X-Ray Diffraction
Publicat a: Scientific reports (Nature Publishing Group), Vol. 7 (2017) , art. 16994, ISSN 2045-2322

DOI: 10.1038/s41598-017-17259-4
PMID: 29208936


16 p, 3.8 MB

El registre apareix a les col·leccions:
Documents de recerca > Documents dels grups de recerca de la UAB > Centres i grups de recerca (producció científica) > Ciències de la salut i biociències > Institut de Biotecnologia i de Biomedicina (IBB)
Articles > Articles de recerca
Articles > Articles publicats

 Registre creat el 2020-06-22, darrera modificació el 2021-05-05



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