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NATs at a glance
Henriette Aksnes1, Nina McTiernan1, Thomas Arnesen1,2,3
1Department of Biomedicine, University of Bergen, 5009 Bergen, Norway.
N-terminal acetylation, a common protein modification by N-terminal acetyltransferases (NATs), impacts protein function and cellular processes. Genetic studies highlight its critical roles in human health and disease.
Area of Science:
- Biochemistry
- Molecular Biology
- Human Physiology
Background:
- Most proteins undergo N-terminal acetylation co-translationally via N-terminal acetyltransferases (NATs).
- This modification influences protein functionality and cellular processes.
- Defects in N-terminal acetylation are linked to various human diseases.
Purpose of the Study:
- To provide an overview of human N-terminal acetyltransferase (NAT) enzymes.
- To describe NAT properties, substrate specificity, and cellular functions.
- To explore the connections between NATs and human pathology.
Main Methods:
- Literature review of N-terminal acetylation.
- Analysis of N-terminal acetyltransferase (NAT) enzyme properties.
- Examination of genetic studies linking N-terminal acetylation to disease.
Main Results:
- Human NAT enzymes exhibit diverse properties and substrate specificities.
- N-terminal acetylation plays essential roles in fundamental cellular processes.
- Dysregulation of N-terminal acetylation is implicated in human diseases.
Conclusions:
- N-terminal acetylation is a vital post-translational modification with significant physiological and pathological implications.
- Understanding human NAT enzymes is crucial for deciphering their roles in health and disease.
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