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

• DOI: 10.1074/jbc.m117.788588
• Publication Date: 2017-08-19T00:25:24Z
• Authors: Fernando Gomes; Flávio Romero Palma; Mario H. Barros; Eduardo T. Tsuchida; Helena G. Turano; Thiago G.P. Alegria; Marilene Demasi; Luis E.S. Netto
• Keywords: Intermembrane space; Mitochondrial carrier; Mitochondrial matrix; Peroxiredoxin; Mitochondrial intermembrane space; Inner membrane

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