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.
Dates
Type | When |
---|---|
Created | 21 years, 3 months ago (May 14, 2004, 8:18 p.m.) |
Deposited | 2 years, 1 month ago (July 21, 2023, 9:57 p.m.) |
Indexed | 3 months, 1 week ago (May 20, 2025, 9:07 p.m.) |
Issued | 33 years, 8 months ago (Dec. 15, 1991) |
Published | 33 years, 8 months ago (Dec. 15, 1991) |
Published Online | 33 years, 8 months ago (Dec. 15, 1991) |
Published Print | 33 years, 8 months ago (Dec. 15, 1991) |
@article{Wienhues_1991, title={Protein folding causes an arrest of preprotein translocation into mitochondria in vivo.}, volume={115}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.115.6.1601}, DOI={10.1083/jcb.115.6.1601}, number={6}, journal={The Journal of cell biology}, publisher={Rockefeller University Press}, author={Wienhues, U and Becker, K and Schleyer, M and Guiard, B and Tropschug, M and Horwich, A L and Pfanner, N and Neupert, W}, year={1991}, month=dec, pages={1601–1609} }