Saccharomyces cerevisiae malate dehydrogenase Mdh1p lacking mitochondrial targeting signal can be re-localized to peroxisomes.

ABSTRACT: Yeast mitochondrial malate dehydrogenase, Mdh1p, is known to form supramolecular complexes with other tricarboxylic acid (TCA) cycle and mitochondrial dehydrogenase enzymes, including the aldehyde dehydrogenase, Ald4p. These complexes have been proposed to facilitate NADH channeling. Here, we demonstrate that in cells grown to saturation and stationary phases, the endogenous Mdh1p, expressed without its mitochondrial targeting signal (MTS), stays outside mitochondria, in both a diffuse cytoplasmic distribution and localized to distinct puncta. The puncta formed by MTS-lacking Mdh1p show no co-localization with the MTS-lacking Ald4p, suggesting that they do not co-assemble into a supramolecular complex in the cytoplasm. However, we found that the MTS-lacking Mdh1p does co-localize with its

SUBMITTER: Chan C 

PROVIDER: S-EPMC12505276 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature