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Molecular and Cellular Biology, October 2001, p. 7097-7104, Vol. 21, No. 20
Institut für Biochemie und
Molekularbiologie1 and Fakultät
für Biologie,2 Universität Freiburg,
D-79104 Freiburg, and Institut für Mikrobiologie,
Universität Hohenheim, D-70593 Stuttgart,3
Germany
Received 9 March 2001/Returned for modification 12 April
2001/Accepted 19 July 2001
The mitochondrial heat shock protein Hsp70 (mtHsp70) is essential
for driving translocation of preproteins into the matrix. Two models,
trapping and pulling by mtHsp70, are discussed, but positive evidence
for either model has not been found so far. We have analyzed a mutant
mtHsp70, Ssc1-2, that shows a reduced interaction with the membrane
anchor Tim44, but an enhanced trapping of preproteins. Unexpectedly, at
a low inner membrane potential, ssc1-2 mitochondria
imported loosely folded preproteins more efficiently than wild-type
mitochondria. The import of a tightly folded preprotein, however, was
not increased in ssc1-2 mitochondria. Thus, enhanced trapping by mtHsp70 stimulates the import of loosely folded preproteins and reduces the dependence on the import-driving activity of the membrane potential, directly demonstrating that trapping is one of the
molecular mechanisms of mtHsp70 action.
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.20.7097-7104.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Mitochondrial Import Driving Forces: Enhanced
Trapping by Matrix Hsp70 Stimulates Translocation and Reduces the
Membrane Potential Dependence of Loosely Folded Preproteins
*
Corresponding author. Mailing address: Institut
für Biochemie und Molekularbiologie, Universität
Freiburg, Hermann-Herder-Strasse 7, Universität Freiburg,
D-79104 Freiburg, Germany. Phone: 49-761-203-5269. Fax:
49-761-203-5261. E-mail: voos{at}ruf.uni-freiburg.de.
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