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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments

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Author(s):
Gomes, Fernando [1] ; Palma, Flavio Romero [1] ; Barros, Mario H. [2] ; Tsuchida, Eduardo T. [1] ; Turano, Helena G. [2] ; Alegria, Thiago G. P. [1] ; Demasi, Marilene [3] ; Netto, Luis E. S. [1]
Total Authors: 8
Affiliation:
[1] Univ Sao Paulo, Inst Biociencias, Dept Genet & Biol Evolut, BR-05508090 Sao Paulo - Brazil
[2] Univ Sao Paulo, Inst Ciencias Biomed, Dept Microbiol, BR-05508900 Sao Paulo - Brazil
[3] Inst Butantan, Lab Bioquim & Biofis, BR-05503001 Sao Paulo - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Journal of Biological Chemistry; v. 292, n. 41, p. 17011-17024, OCT 13 2017.
Web of Science Citations: 4
Abstract

Yeast Prx1 is a mitochondrial 1-Cys peroxiredoxin that catalyzes the reduction of endogenously generated H2O2. Prx1 is synthesized on cytosolic ribosomes as a preprotein with a cleavable N-terminal presequence that is the mitochondrial targeting signal, but the mechanisms underlying Prx1 distribution to distinct mitochondrial subcompartments are unknown. Here, we provide direct evidence of the following dual mitochondrial localization of Prx1: a soluble form in the intermembrane space and a form in the matrix weakly associated with the inner mitochondrial membrane. We show that Prx1 sorting into the intermembrane space likely involves the release of the protein precursor within the lipid bilayer of the inner membrane, followed by cleavage by the inner membrane peptidase. We also found that during its import into the matrix compartment, Prx1 is sequentially cleaved by mitochondrial processing peptidase and then by octapeptidyl aminopeptidase 1 (Oct1). Oct1 cleaved eight amino acid residues from the N-terminal region of Prx1 inside the matrix, without interfering with its peroxidase activity in vitro. Remarkably, the processing of peroxiredoxin (Prx) proteins by Oct1 appears to be an evolutionarily conserved process because yeast Oct1 could cleave the human mitochondrial peroxiredoxin Prx3 when expressed in Saccharomyces cerevisiae. Altogether, the processing of peroxiredoxins by Imp2 or Oct1 likely represents systems that control the localization of Prxs into distinct compartments and thereby contribute to various mitochondrial redox processes. (AU)

FAPESP's process: 13/07937-8 - Redoxome - Redox Processes in Biomedicine
Grantee:Ohara Augusto
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 12/21722-1 - Structural and biochemical characterization of Ohr/OsmC family proteins: emphasis on the characterization of a Francisella tularensis protein involved in pathogenicity
Grantee:Diogo de Abreu Meireles
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 08/07971-3 - Kinetic characterization and search for inhibitors of Ohr (Organic Hydroperoxide Resistance Protein) from Xylella fastidiosa
Grantee:Thiago Geronimo Pires Alegria
Support type: Scholarships in Brazil - Master