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Published online September 24, 2007
doi:10.1083/jcb.200706195
The Journal of Cell Biology, Vol. 178, No. 7, 1161-1175
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Hwang et al.
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Article

Tim54p connects inner membrane assembly and proteolytic pathways in the mitochondrion



David K. Hwang1, Steven M. Claypool1, Danielle Leuenberger1, Heather L. Tienson1, and Carla M. Koehler1,2,3

1 Department of Chemistry and Biochemistry, 2 Jonsson Comprehensive Cancer Center, and 3 Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095

Correspondence to Carla M. Koehler: koehler{at}chem.ucla.edu

Tim54p, a component of the inner membrane TIM22 complex, does not directly mediate the import of inner membrane substrates but is required for assembly/stability of the 300-kD TIM22 complex. In addition, {Delta}tim54 yeast exhibit a petite-negative phenotype (also observed in yeast harboring mutations in the F1Fo ATPase, the ADP/ATP carrier, mitochondrial morphology components, or the i–AAA protease, Yme1p). Interestingly, other import mutants in our strain background are not petite-negative. We report that Tim54p is not involved in maintenance of mitochondrial DNA or mitochondrial morphology. Rather, Tim54p mediates assembly of an active Yme1p complex, after Yme1p is imported via the TIM23 pathway. Defective Yme1p assembly is likely the major contributing factor for the petite-negativity in strains lacking functional Tim54p. Thus, Tim54p has two independent functions: scaffolding/stability for the TIM22 membrane complex and assembly of Yme1p into a proteolytically active complex. As such, Tim54p links protein import, assembly, and turnover pathways in the mitochondrion.

D. Leuenberger's present address is Department of Biology and Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305-5439.

Abbreviations used in this paper: TIM, translocons of the inner membrane; TOM, translocons of the outer membrane; WT, wild type.


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