spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Schleiff, E.
Right arrow Articles by McBride, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schleiff, E.
Right arrow Articles by McBride, H.

Journal of Cell Science, Vol 113, Issue 12 2267-2272, Copyright © 2000 by Company of Biologists

JOURNAL ARTICLES

The central matrix loop drives import of uncoupling protein 1 into mitochondria

E Schleiff and H McBride
Department of Biochemistry, McGill University Montreal, Montreal, Canada, H3G 1Y6. eschleiff@bot.uni-kiel.de

The uncoupling protein (UCP1) is a carrier protein of the inner mitochondrial membrane spanning the bilayer six times. It does not contain a typical amino-terminal targeting signal and the mechanism of targeting and insertion is unknown. Here we focus on the biogenesis of UCP1 by analysing the import signals contained within the three repeated units of the protein. The amino-terminal third of the protein can mediate insertion into the outer membrane and therefore acts as artificial targeting signal when fused to DHFR. However, in the context of full-length UCP, the targeting information contained within the first repeated unit is not sufficient to trigger insertion into the outer membrane. Deletion of either the first or third repeated unit from UCP1 did not reduce import into the inner membrane and bound to the outer membrane receptor protein hTom20 with the characteristics of full-length UCP1. Deletion of the second repeat of UCP1 completely abolished all import into the mitochondria. Consistent with this, the central repeat alone was efficiently imported to the inner membrane and bound hTom20 with the characteristics of UCP1. We conclude that the site for binding hTom20 is within the central repeat and that this domain contains the complete targeting signal for directing UCP1 to the inner membrane.


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
L. Shen, J. Guo, C. Santos-Berrios, and M. X. Wu
Distinct Domains for Anti- and Pro-apoptotic Activities of IEX-1
J. Biol. Chem., June 2, 2006; 281(22): 15304 - 15311.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Brandner, P. Rehling, and K. N. Truscott
The Carboxyl-terminal Third of the Dicarboxylate Carrier Is Crucial for Productive Association with the Inner Membrane Twin-pore Translocase
J. Biol. Chem., February 18, 2005; 280(7): 6215 - 6221.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
S. P. Curran, D. Leuenberger, E. Schmidt, and C. M. Koehler
The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins
J. Cell Biol., September 16, 2002; 158(6): 1017 - 1027.
[Abstract] [Full Text] [PDF]

Home page
 J. Appl. Physiol.Home page
G. Argyropoulos and M.-E. Harper
Molecular Biology of Thermoregulation: Invited Review: Uncoupling proteins and thermoregulation
J Appl Physiol, May 1, 2002; 92(5): 2187 - 2198.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2000