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Titolo:
PTS2 protein import into mammalian peroxisomes
Autore:
Legakis, JE; Terlecky, SR;
Indirizzi:
Wayne State Univ, Sch Med, Dept Pharmacol, Detroit, MI 48201 USA Wayne State Univ Detroit MI USA 48201 pt Pharmacol, Detroit, MI 48201 USA
Titolo Testata:
TRAFFIC
fascicolo: 4, volume: 2, anno: 2001,
pagine: 252 - 260
SICI:
1398-9219(200104)2:4<252:PPIIMP>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
RHIZOMELIC CHONDRODYSPLASIA PUNCTATA; OVARY CELL MUTANT; TARGETING SIGNAL; 3-KETOACYL-COA THIOLASE; RECEPTOR DOCKING; LONGER ISOFORM; HUMAN PEX7; PEX14P; BIOGENESIS; DISORDERS;
Keywords:
chaperone; peroxin; peroxisome; protein import; thiolase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Terlecky, SR Wayne State Univ, Sch Med, Dept Pharmacol, 540 E Canfield Ave, Detroit, MI48201 USA Wayne State Univ 540 E Canfield Ave Detroit MI USA 48201 USA
Citazione:
J.E. Legakis e S.R. Terlecky, "PTS2 protein import into mammalian peroxisomes", TRAFFIC, 2(4), 2001, pp. 252-260

Abstract

Peroxisome targeting signal (PTS)2 directs proteins from their site of synthesis in the cytosol to the lumen of the peroxisome. Unlike PTS1 which is present in the great majority of peroxisomal matrix proteins and whose import mechanics have been dissected in considerable detail, PTS2 is a relatively rare topogenic signal whose import mechanisms are far less well understood. However, as is the case for PTS1 proteins, an inability to import PTS2 proteins leads to human disease. In this report, we describe the biochemical characterization of mammalian PTS2 protein import using a semi-permeabilized cell system. We show that a PTS2-containing reporter molecule is taken up by peroxisomes in a reaction that is time-, temperature-, ATP-, and cytosol-dependent. Furthermore, the import process is specific, saturable, and requires action of the chaperone Hsc70, the cochaperone Hsp40, and the peroxins Pex5p and Pex14p. We also demonstrate peroxisomal translocation of PTS2 reporter/antibody complexes confirming the import competence of higher order structures. Importantly, cultured fibroblasts from patients with the rhizomelic form of chondrodysplasia punctata (RCDP) which are deficient for the PTS2 receptor protein, Pex7p, are unable to import the PTS2 reporter in this assay. The ability to monitor PTS2 import in vitro will permit, for the first time, a detailed comparison of the biochemical properties of PTS1 and PTS2 protein import.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 05:25:37