Saccharomyces cerevisiae malate dehydrogenase Mdh1p lacking mitochondrial targeting signal can be re-localized to peroxisomes
3
Issued Date
2025-09-01
Resource Type
eISSN
20466390
Scopus ID
2-s2.0-105018683063
Journal Title
Biology Open
Volume
14
Issue
9
Rights Holder(s)
SCOPUS
Bibliographic Citation
Biology Open Vol.14 No.9 (2025)
Suggested Citation
Chan C., Sirinonthanawech N., Sato B.K., Wilhelm J.E., Noree C. Saccharomyces cerevisiae malate dehydrogenase Mdh1p lacking mitochondrial targeting signal can be re-localized to peroxisomes. Biology Open Vol.14 No.9 (2025). doi:10.1242/bio.062199 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/112713
Title
Saccharomyces cerevisiae malate dehydrogenase Mdh1p lacking mitochondrial targeting signal can be re-localized to peroxisomes
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Corresponding Author(s)
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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 cytoplasmic counterpart, Mdh2p, in puncta. Interestingly, Mdh2p has recently been reported to form heterocomplexes with the peroxisomal Mdh3p and to be transported into peroxisomes to assist in the glyoxylate cycle. We also show that the MTS-lacking Mdh1p co-localizes with a fluorescent peroxisome marker, Pex3p. Our findings suggest that different malate dehydrogenases can enter peroxisomes, potentially as a means to make the glyoxylate pathway more efficient.