Overproduction of PDR3 suppresses mitochondrial import defects associated with a TOM70 null mutation by increasing the expression of TOM72 in Saccharomyces cerevisiae

Molecular and Cellular Biology
J Y KohD M Bedwell

Abstract

Most mitochondrial proteins are synthesized with cleavable amino-terminal targeting signals that interact with the mitochondrial import machinery to facilitate their import from the cytosol. We previously reported that the presequence of the F(1)-ATPase beta subunit precursor (pre-F(1)beta) acts as an intramolecular chaperone that maintains the precursor in an import-competent conformation prior to import (P. Hajek, J. Y. Koh, L. Jones, and D. M. Bedwell, Mol. Cell. Biol. 17:7169-7177, 1997). We also found that a mutant form of pre-F(1)beta with a minimal targeting signal (Delta 1,2 pre-F(1)beta) is inefficiently imported into mitochondria because it rapidly folds into an import-incompetent conformation. We have now analyzed the consequences of reducing the pre-F(1)beta targeting signal to a minimal unit in more detail. We found that Delta 1,2 pre-F(1)beta is more dependent upon the Tom70p receptor for import than WT pre-F(1)beta is, resulting in a growth defect on a nonfermentable carbon source at 15 degrees C. Experiments using an in vitro mitochondrial protein import system suggest that Tom70p functions to maintain a precursor containing the Delta 1,2 pre-F(1)beta import signal in an import-competent conformation. We also id...Continue Reading

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Citations

Sep 9, 2010·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Jingzhi LiBingdong Sha
Mar 7, 2020·Biological Chemistry·Thomas BauseweinStephan Nussberger
Apr 1, 2004·The Plant Journal : for Cell and Molecular Biology·Diane ConstanPaul Jarvis
Oct 7, 2020·International Journal of Molecular Sciences·Sebastian Kreimendahl, Joachim Rassow

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