Publication: Coupled regulations of enzymatic activity and structure formation of aldehyde dehydrogenase Ald4p
Issued Date
2020-04-01
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ISSN
20466390
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2-s2.0-85086173775
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Mahidol University
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SCOPUS
Bibliographic Citation
Biology Open. Vol.9, No.4 (2020)
Suggested Citation
Chalongrat Noree, Naraporn Sirinonthanawech Coupled regulations of enzymatic activity and structure formation of aldehyde dehydrogenase Ald4p. Biology Open. Vol.9, No.4 (2020). doi:10.1242/bio.051110 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/57611
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Title
Coupled regulations of enzymatic activity and structure formation of aldehyde dehydrogenase Ald4p
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Abstract
© 2020. Published by The Company of Biologists Ltd Previously, we have developed an extramitochondrial assembly system, where mitochondrial targeting signal (MTS) can be removed from a given mitochondrial enzyme, which could be used to characterize the regulatory factors involved in enzyme assembly/ disassembly in vivo. Here, we demonstrate that addition of exogenous acetaldehyde can quickly induce the supramolecular assembly of MTS-deleted aldehyde dehydrogenase Ald4p in yeast cytoplasm. Also, by using PCR-based modification of the yeast genome, cytoplasmically targeted Ald4p cannot polymerize into long filaments when key functional amino acid residues are substituted, as shown by N192D, S269A, E290K and C324A mutations. This study has confirmed that extramitochondrial assembly could be a powerful external system for studying mitochondrial enzyme assembly, and its regulatory factors outside the mitochondria. In addition, we propose that mitochondrial enzyme assembly/disassembly is coupled to the regulation of a given mitochondrial enzyme activity.