Localization and regulation of yeast aldehyde dehydrogenase Ald4p structures
Previously, we identified yeast strains, namely SWORD, showing more robust Ald4p-GFP filament formation than the typical <i>ALD4::GFP</i> 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.
Authors
- James E. Wilhelm (ORCID: https://orcid.org/0000-0001-5082-4532)
- Naraporn Sirinonthanawech (ORCID: https://orcid.org/0000-0002-7870-7706)
- Chalongrat Noree (ORCID: https://orcid.org/0000-0002-7774-4281)
- Brian K. Sato
- Channarong Nasalingkhan (ORCID: https://orcid.org/0009-0007-4115-3408)
Institutions
- University of California, Irvine (US)
- Mahidol University (TH)
- University of California San Diego (US)
Publication Details
- Journal
- Heliyon
- Published
- 2024-10-01
- DOI
- https://doi.org/10.1016/j.heliyon.2024.e39048
- Citations
- 1
- Primary Topic
- Biochemical and Molecular Research
- Type
- article
- Field-Weighted Citation Impact
- 0.23
Funders
- Mahidol University