Localization and regulation of yeast aldehyde dehydrogenase Ald4p structures
Channarong Nasalingkhan,
Naraporn Sirinonthanawech,
Brian K. Sato,
James E. Wilhelm,
Chalongrat Noree
Affiliations
Channarong Nasalingkhan
Institute of Molecular Biosciences, Mahidol University 25/25 Phuttamonthon 4 Road, Salaya, Phuttamonthon, Nakhon Pathom, 73170, Thailand
Naraporn Sirinonthanawech
Institute of Molecular Biosciences, Mahidol University 25/25 Phuttamonthon 4 Road, Salaya, Phuttamonthon, Nakhon Pathom, 73170, Thailand
Brian K. Sato
Department of Molecular Biology and Biochemistry, Charlie Dunlop School of Biological Sciences, University of California, Irvine, 2238 McGaugh Hall, Irvine, CA, 92697, USA
James E. Wilhelm
Section of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, 9500 Gilman Drive (MC0347), La Jolla, CA, 92093-0347, USA
Chalongrat Noree
Institute of Molecular Biosciences, Mahidol University 25/25 Phuttamonthon 4 Road, Salaya, Phuttamonthon, Nakhon Pathom, 73170, Thailand; Corresponding author.
Previously, we identified yeast strains, namely SWORD, showing more robust Ald4p-GFP filament formation than the typical ALD4::GFP strains. Here, we report that Ald4p-GFP in SWORD strains favorably polymerize into gigantic structures in the cytoplasm, despite the enzyme being established as a mitochondrial resident. In addition, we have found that nocodazole, a microtubule destabilizer, has no effect on Ald4p high-order assembly, suggesting no direct association between microtubule dynamics and Ald4p structure formation. Ald4p assembly cannot be induced by sodium azide treatment, indicating that ATP is not a primary effector of Ald4p polymerization. Interestingly, addition of exogenous acetaldehyde, a substrate of the enzyme, can significantly enhance the structure formation of Ald4p, implying that structure formation may be related to enzymatic activity.
