Protein unfolding by mitochondria - The Hsp70 import motor

Citation
A. Matouschek et al., Protein unfolding by mitochondria - The Hsp70 import motor, EMBO REP, 1(5), 2000, pp. 404-410
Citations number
59
Categorie Soggetti
Molecular Biology & Genetics
Journal title
EMBO REPORTS
ISSN journal
1469221X → ACNP
Volume
1
Issue
5
Year of publication
2000
Pages
404 - 410
Database
ISI
SICI code
1469-221X(200011)1:5<404:PUBM-T>2.0.ZU;2-U
Abstract
Protein unfolding is a key step in the import of some proteins into mitocho ndria and chloroplasts and in the degradation of regulatory proteins by ATP -dependent proteases. In contrast to protein folding, the reverse process h as remained largely uninvestigated until now. This review discusses recent discoveries on the mechanism of protein unfolding during translocation into mitochondria. The mitochondria can actively unfold preproteins by unraveli ng them from the N-terminus. The central component of the mitochondrial imp ort motor, the matrix heat shock protein 70, functions by bath pulling and holding the preproteins.