Arabidopsis thaliana Hcc1 is a Sco-like metallochaperone for Cu A assembly in Cytochrome c Oxidase.

Autor: Llases ME; Instituto de Biología Molecular y Celular de Rosario (IBR CONICET-UNR), Rosario, Argentina., Lisa MN; Instituto de Biología Molecular y Celular de Rosario (IBR CONICET-UNR), Rosario, Argentina.; Plataforma de Biología Estructural y Metabolómica (PLABEM), Rosario, Argentina., Morgada MN; Instituto de Biología Molecular y Celular de Rosario (IBR CONICET-UNR), Rosario, Argentina.; Area Biofísica, Departamento de Química Biológica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Argentina., Giannini E; Instituto de Biología Molecular y Celular de Rosario (IBR CONICET-UNR), Rosario, Argentina., Alzari PM; Unité de Microbiologie Structurale, Institut Pasteur, Université Paris Diderot, Paris, France., Vila AJ; Instituto de Biología Molecular y Celular de Rosario (IBR CONICET-UNR), Rosario, Argentina.; Plataforma de Biología Estructural y Metabolómica (PLABEM), Rosario, Argentina.; Area Biofísica, Departamento de Química Biológica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Argentina.
Jazyk: angličtina
Zdroj: The FEBS journal [FEBS J] 2020 Feb; Vol. 287 (4), pp. 749-762. Date of Electronic Publication: 2019 Aug 07.
DOI: 10.1111/febs.15016
Abstrakt: The assembly of the Cu A site in Cytochrome c Oxidase (COX) is a critical step for aerobic respiration in COX-dependent organisms. Several gene products have been associated with the assembly of this copper site, the most conserved of them belonging to the Sco family of proteins, which have been shown to perform different roles in different organisms. Plants express two orthologs of Sco proteins: Hcc1 and Hcc2. Hcc1 is known to be essential for plant development and for COX maturation, but its precise function has not been addressed until now. Here, we report the biochemical, structural and functional characterization of Arabidopsis thaliana Hcc1 protein (here renamed Sco1). We solved the crystal structure of the Cu +1 -bound soluble domain of this protein, revealing a tri coordinated environment involving a CxxxCx n H motif. We show that AtSco1 is able to work as a copper metallochaperone, inserting two Cu +1 ions into the Cu A site in a model of CoxII. We also show that AtSco1 does not act as a thiol-disulfide oxido-reductase. Overall, this information sheds new light on the biochemistry of Sco proteins, highlighting the diversity of functions among them despite their high structural similarities. DATABASE: PDB entry 6N5U (Crystal structure of Arabidopsis thaliana ScoI with copper bound).
(© 2019 Federation of European Biochemical Societies.)
Databáze: MEDLINE
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