Busca avançada
Ano de início
Entree
(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

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

Texto completo
Autor(es):
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]
Número total de Autores: 8
Afiliação do(s) autor(es):
[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
Número total de Afiliações: 3
Tipo de documento: Artigo Científico
Fonte: Journal of Biological Chemistry; v. 292, n. 41, p. 17011-17024, OCT 13 2017.
Citações Web of Science: 4
Resumo

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)

Processo FAPESP: 13/07937-8 - Redoxoma
Beneficiário:Ohara Augusto
Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs
Processo FAPESP: 12/21722-1 - Caracterização estrutural e bioquímica de proteínas da família Ohr/OsmC: ênfase para a caracterização de uma proteína de Francisella tularensis envolvida em patogenicidade
Beneficiário:Diogo de Abreu Meireles
Linha de fomento: Bolsas no Brasil - Pós-Doutorado
Processo FAPESP: 08/07971-3 - Caracterização cinética e busca de inibidores de Ohr (organic hydroperoxide Resistence Protein)de Xylella fastidiosa
Beneficiário:Thiago Geronimo Pires Alegria
Linha de fomento: Bolsas no Brasil - Mestrado