Abstract
Precise targeting of mitochondrial proteins to the target organelles requires recognition of mitochondrial-targeting signals encoded in the proteins themselves by receptor proteins including Tom20 and Tom70 on the mitochondrial surface. We analyzed interactions between mitochondrial presequences and their receptors, Tom20 and Tom22, with NMR. Based on the NMR results, we propose that a presequence contains multiple signals for distinct presequence binding proteins along the import pathway. In vitro import of the translation products of the yeast total mRNA into isolated mitochondria with and without Tom70 followed by 2D electrophoresis and radioimaging allowed us to identify many substrate proteins for recognition by Tom70, a receptor mainly for presequence-less polytopic membrane proteins.
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