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Protein arginylation regulates cellular stress response by stabilizing HSP70 and HSP40 transcripts
Kamalakshi Deka1, Archana Singh1, Surajit Chakraborty1
1Department of Molecular Biology and Biotechnology, Tezpur University , Napaam, Assam, India.
Cell Death Discovery
|October 19, 2016
Summary
Arginylation, a protein modification, protects cells from heat stress. Loss of the enzyme Arginyltransferase 1 (ATE1) increases heat sensitivity by impairing heat-shock protein expression and mRNA stability.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Stress Response
Background:
- Arginylation, a post-translational modification mediated by Arginyltransferase 1 (ATE1), regulates protein function and stability.
- Arginylation is implicated in various cellular stress conditions, but its specific role in heat stress response remains unclear.
Purpose of the Study:
- To investigate the role of arginylation in cellular response to heat stress.
- To determine the impact of ATE1 deficiency on heat stress susceptibility and associated molecular mechanisms.
Main Methods:
- Comparison of wild-type and Ate1 knockout (KO) cells under heat stress conditions.
- Analysis of apoptosis induction, gene expression of heat-shock proteins (HSP70.1, HSP70.3, HSP40), and mRNA stability.
- Assessment of phenotype rescue by Ate1 overexpression in KO cells.
Main Results:
- Ate1 KO cells exhibited increased susceptibility to heat stress, characterized by enhanced apoptosis.
- Heat shock protein gene expression was initially induced but diminished later in KO cells.
- Loss of ATE1 significantly reduced the stability of HSP70.1, HSP70.3, and HSP40 mRNAs.
- Overexpression of Ate1 restored normal heat stress response phenotypes in KO cells.
Conclusions:
- Arginylation plays a crucial protective role in cellular heat stress response.
- ATE1 regulates heat stress tolerance by modulating heat-shock protein gene expression and mRNA stability.
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