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Titolo:
A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation
Autore:
Sevier, CS; Cuozzo, JW; Vala, A; Aslund, F; Kaiser, CA;
Indirizzi:
MIT, Dept Biol, Cambridge, MA 02139 USA MIT Cambridge MA USA 02139MIT, Dept Biol, Cambridge, MA 02139 USA
Titolo Testata:
NATURE CELL BIOLOGY
fascicolo: 10, volume: 3, anno: 2001,
pagine: 874 - 882
SICI:
1465-7392(200110)3:10<874:AFODAN>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-DISULFIDE-ISOMERASE; SACCHAROMYCES-CEREVISIAE; LIVER-REGENERATION; YEAST SCERV1; ACTIVE-SITE; GENE; GROWTH; IDENTIFICATION; THIOREDOXIN; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Kaiser, CA MIT, Dept Biol, 77 Massachusetts Ave, Cambridge, MA 02139 USA MIT 77 Massachusetts Ave Cambridge MA USA 02139 e, MA 02139 USA
Citazione:
C.S. Sevier et al., "A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation", NAT CELL BI, 3(10), 2001, pp. 874-882

Abstract

Ero1 and Pdi1 are essential elements of the pathway for the formation of disulphide bonds within the endoplasmic reticulum (ER). By screening for alternative oxidation pathways in Saccharomyces cerevisiae, we identified EM as a gene that when overexpressed can restore viability and disulphide bond formation to an ero1-1 mutant strain. EM encodes a luminal ER protein of relative molecular mass 22,000. Purified recombinant Erv2p is a flavoenzyme that can catalyse O-2-dependent formation of disulphide bonds. Erv2p transfers oxidizing equivalents to Pdi1p by a dithiol-disulphide exchange reaction, indicating that the Erv2p-dependent pathway for disulphide bond formationclosely parallels that of the previously identified Ero1p-dependent pathway.

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Documento generato il 01/04/20 alle ore 20:46:26