Study of the molecular pathways of protein import in mitochondria
Abstract
Erv1 and Mia40 constitute the two important components of the disulfide relay system that mediates oxidative protein folding of the small Tim proteins and other cysteine rich substrates in the mitochondrial intermembrane space. The small Tims chaperone hydrophobic precursors across the mitochondrial intermembrane space. Tim9 and Tim10 form the soluble TIM10 complex that binds precursors exiting from the outer membrane. Tim12 functions downstream, as the only small Tim peripherally attached on the inner membrane. The aim of the first part of this study was to investigate the funvtion that renders Tim12 essential for the cell, and the domain via which it is mediated. It is shown that Tim12 has an intrinsic affinity for the lipids of the inner mitochondrial membrane. The C-terminal end of Tim12 is essential in vivo and it determines the interaction with the membrane and the assembly of the protein in complexes with the other Tims. The N-terminal end, is dispensable and it both contains ta ...
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