|
||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
J. Cell Biol.,
Volume 145, Number 5, May 31, 1999 961-972


* Institut für Biochemie und Molekularbiologie, Universität Freiburg, D-79104 Freiburg, Germany; and Tim44 is a protein of the mitochondrial inner
membrane and serves as an adaptor protein for
mtHsp70 that drives the import of preproteins in an
ATP-dependent manner. In this study we have modified the interaction of Tim44 with mtHsp70 and characterized the consequences for protein translocation. By
deletion of an 18-residue segment of Tim44 with limited
similarity to J-proteins, the binding of Tim44 to
mtHsp70 was weakened. We found that in the yeast
Saccharomyces cerevisiae the deletion of this segment is
lethal. To investigate the role of the 18-residue segment, we expressed Tim44
Institute for Molecular
Cell Biology, BioCentrum Amsterdam, 1098 SM Amsterdam, The Netherlands
18 in addition to the endogenous
wild-type Tim44. Tim44
18 is correctly targeted to mitochondria and assembles in the inner membrane import
site. The coexpression of Tim44
18 together with wild-type Tim44, however, does not stimulate protein import, but reduces its efficiency. In particular, the promotion of unfolding of preproteins during translocation is
inhibited. mtHsp70 is still able to bind to Tim44
18 in an
ATP-regulated manner, but the efficiency of interaction is reduced. These results suggest that the J-related segment of Tim44 is needed for productive interaction with
mtHsp70. The efficient cooperation of mtHsp70 with
Tim44 facilitates the translocation of loosely folded
preproteins and plays a crucial role in the import of
preproteins which contain a tightly folded domain.
This article has been cited by other articles:
|
|