Localization and regulation of yeast aldehyde dehydrogenase Ald4p structures
Issued Date
2024-10-30
Resource Type
eISSN
24058440
Scopus ID
2-s2.0-85206265955
Journal Title
Heliyon
Volume
10
Issue
20
Rights Holder(s)
SCOPUS
Bibliographic Citation
Heliyon Vol.10 No.20 (2024)
Suggested Citation
Nasalingkhan C., Sirinonthanawech N., Sato B.K., Wilhelm J.E., Noree C. Localization and regulation of yeast aldehyde dehydrogenase Ald4p structures. Heliyon Vol.10 No.20 (2024). doi:10.1016/j.heliyon.2024.e39048 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/101697
Title
Localization and regulation of yeast aldehyde dehydrogenase Ald4p structures
Corresponding Author(s)
Other Contributor(s)
Abstract
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.