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NATs at a glance.

Henriette Aksnes1, Nina McTiernan1, Thomas Arnesen1,2,3

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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.

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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.