Human aldehyde dehydrogenase 3A1 (ALDH3A1) exhibits chaperone-like function
Georgia-Persephoni Voulgaridou1, Ilias Tsochantaridis1, Theodora Mantso2
1Department of Molecular Biology & Genetics, Democritus University of Thrace, University Campus, Dragana, Alexandroupolis 68100, Greece.
Summary
Aldehyde dehydrogenase 3A1 (ALDH3A1) acts as a molecular chaperone, protecting proteins from damage. This enzyme enhances cellular resistance to oxidative and thermal stress, supporting its multifunctional role in cellular homeostasis.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Stress Response
Background:
- Aldehyde dehydrogenase 3A1 (ALDH3A1) is a metabolic enzyme crucial for aldehyde oxidation.
- High ALDH3A1 expression in stress-exposed epithelial tissues suggests a role in maintaining cellular homeostasis.
- ALDH3A1 is known to mediate resistance to cellular oxidative stress through metabolic and non-metabolic functions.
Purpose of the Study:
- To investigate the potential molecular chaperone-like activity of human ALDH3A1.
- To determine if ALDH3A1 can protect proteins from precipitation and deactivation under thermal stress.
- To assess the protective effects of ALDH3A1 against cellular stress in bacterial and human cell models.
Main Methods:
- Human ALDH3A1 was expressed and purified from E. coli.
- In vitro assays were performed using recombinant ALDH3A1 to protect SmaI and citrate synthase from thermal stress.
- ALDH3A1 was overexpressed in E. coli and human corneal epithelial cells (HCE-2) to evaluate stress resistance.
Main Results:
- Recombinant ALDH3A1 demonstrated significant in vitro chaperone function.
- Overexpression of ALDH3A1 in E. coli enhanced resistance to thermal shock.
- ALDH3A1 overexpression in HCE-2 cells protected against hydrogen peroxide and tert-butyl hydroperoxide cytotoxicity.
Conclusions:
- Human ALDH3A1 exhibits molecular chaperone-like activity, protecting proteins from aggregation under stress.
- ALDH3A1 plays a vital role in cellular protection beyond its metabolic functions.
- The findings support ALDH3A1's multifunctional role in maintaining cellular integrity under various stress conditions.
More Related Videos
Related Concept Videos
Molecular Chaperones and Protein Folding
20.5K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
20.5K
Molecular Chaperones and Protein Folding
15.2K
15.2K
Export of Misfolded Proteins out of the ER
5.4K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
5.4K
Bacterial Protein Maturation
633
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
633
Gene Families
10.1K
Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
10.1K
Allosteric Proteins-ATCase
6.7K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
6.7K


