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Titolo:
Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences
Autore:
Taylor, AB; Smith, BS; Kitada, S; Kojima, K; Miyaura, H; Otwinowski, Z; Ito, A; Deisenhofer, J;
Indirizzi:
Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 ward Hughes Med Inst, Dallas, TX 75390 USA Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 ed Ctr, Dept Biochem, Dallas, TX 75390 USA Kyushu Univ, Fac Sci, Dept Chem, Fukuoka 8128581, Japan Kyushu Univ Fukuoka Japan 8128581 Sci, Dept Chem, Fukuoka 8128581, Japan
Titolo Testata:
STRUCTURE
fascicolo: 7, volume: 9, anno: 2001,
pagine: 615 - 625
SICI:
0969-2126(20010703)9:7<615:CSOMPP>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYTOCHROME BC(1) COMPLEX; ELECTRON-DENSITY MAPS; BOVINE HEART-MITOCHONDRIA; PROTEIN IMPORT; PRECURSOR PROTEINS; ALDEHYDE DEHYDROGENASE; SUBSTRATE RECOGNITION; SYNTHETIC PEPTIDE; TRANSITION-STATE; ALPHA-SUBUNIT;
Keywords:
crystal structure; metallopeptidase; mitochondrial signal sequence; substrate complex; zinc binding;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
62
Recensione:
Indirizzi per estratti:
Indirizzo: Deisenhofer, J Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 Inst, Dallas, TX 75390 USA
Citazione:
A.B. Taylor et al., "Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences", STRUCTURE, 9(7), 2001, pp. 615-625

Abstract

Background: Mitochondrial processing peptidase (MPP) is a metalloendopeptidase that cleaves the N-terminal signal sequences of nuclear-encoded proteins targeted for transport from the cytosol to the mitochondria. Mitochondrial signal sequences vary in length and sequence, but each is cleaved at a single specific site by MPP. The cleavage sites typically contain an arginine at position -2 (in the N-terminal portion) from the scissile peptide bondin addition to other distal basic residues, and an aromatic residue at position +1. Mitochondrial import machinery recognizes amphiphilic helical conformations in signal sequences. However, it is unclear how MPP specificallyrecognizes diverse presequence substrates. Results: The crystal structures of recombinant yeast MPP and a cleavage-deficient mutant of MPP complexed with synthetic signal peptides have been determined. MPP is a heterodimer; its alpha and beta subunits are homologous to the core II and core I proteins, respectively, of the ubiquinol-cytochrome c oxidoreductase complex. Crystal structures of two different synthetic substrate peptides cocrystallized with the mutant MPP each show the peptidebound in an extended conformation at the active site. Recognition sites for the arginine at position -2 and the +1 aromatic residue are observed. Conclusions: MPP bound two mitochondrial import presequence peptides in extended conformations in a large polar cavity. The presequence conformationsdiffer from the amphiphilic helical conformation recognized by mitochondrial import components. Our findings suggest that the presequences adopt context-dependent conformations through mitochondrial import and processing, helical for recognition by mitochondrial import machinery and extended for cleavage by the main processing component.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 05:29:36