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Type I signal peptidases in the endoplasmic reticulum and mitochondria
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Type I signal peptidases in the endoplasmic reticulum and mitochondria
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Dissertation
Type I signal peptidases in the endoplasmic reticulum and mitochondria
2004
Overview
Type I signal peptidases (SPs) are multisubunit protein complexes with two catalytic subunits in the endoplasmic reticulum (ER) and mitochondria. Here I tested the prevailing hypothesis that SPC18 and SPC21 of mammalian ER SP exhibit nonoverlapping substrate specificity by expressing these catalytic subunits individually in yeast cells. Surprisingly, my results reveal a mechanism of overlapping substrate specificity, although SPC18 and SPC21 differ in catalytic efficiency in a substrate-dependent manner. I have also addressed the functional role of Som1p, the non-catalytic subunit of the inner membrane protease (IMP) in yeast mitochondria. The data suggest that Som1p improves IMP catalytic efficiency, thereby ensuring IMP function before its substrates assume a conformation incompatible with signal peptide cleavage.
