Protein folding causes an arrest of preprotein translocation into mitochondria in vivo.
J Cell Biol
; 115(6): 1601-9, 1991 Dec.
Article
em En
| MEDLINE
| ID: mdl-1757464
ABSTRACT
With vital yeast cells, a hybrid protein consisting of the amino-terminal third of the precursor to cytochrome b2 and of the entire dihydrofolate reductase was arrested on the import pathway into mitochondria. Accumulation of the protein in the mitochondrial membranes was achieved by inducing a stable tertiary structure of the dihydrofolate reductase domain. Thereby, three salient features of mitochondrial protein uptake in vivo were demonstrated its posttranslational character; the requirement for unfolding of precursors; and import through translocation contact sites. The permanent occupation of translocation sites by the fusion protein inhibited the import of other precursors; it did, however, not lead to leakage of mitochondrial ions, implying the existence of a channel that is sealed around the membrane spanning polypeptide segment.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Precursores de Proteínas
/
Mitocôndrias
Tipo de estudo:
Etiology_studies
Idioma:
En
Ano de publicação:
1991
Tipo de documento:
Article