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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
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Spotlight on protein N-terminal acetylation
Rasmus Ree1,2,3, Sylvia Varland1,2,4, Thomas Arnesen5,6,7
1Department of Biological Sciences, University of Bergen, Thormøhlensgate 55, N-5020, Bergen, Norway.
Experimental & Molecular Medicine
|July 29, 2018
Summary
N-terminal acetylation (Nt-acetylation) is a crucial protein modification affecting protein lifespan and properties. This review covers eukaryotic N-terminal acetyltransferases (NATs), their impact, and study methods.
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- N-terminal acetylation (Nt-acetylation) is a prevalent post-translational modification in both eukaryotes and prokaryotes.
- This modification irreversibly alters the N-terminus charge, hydrophobicity, and size, impacting protein characteristics.
- Nt-acetylation influences protein lifespan, folding, and binding affinities.
Purpose of the Study:
- To provide a comprehensive overview of eukaryotic N-terminal acetyltransferases (NATs).
- To elucidate the functional impact of Nt-acetylation on proteins.
- To discuss additional roles of known NATs and present methodologies for studying Nt-acetylation.
Main Methods:
- Literature review of existing research on N-terminal acetylation and NATs.
- Synthesis of information regarding the enzymatic machinery and biological consequences of Nt-acetylation.
- Outline of experimental techniques applicable to the study of Nt-acetylation.
Main Results:
- Eukaryotic NATs are responsible for catalyzing Nt-acetylation.
- Nt-acetylation significantly affects protein stability, folding, and molecular interactions.
- Known NATs possess diverse functions beyond their primary catalytic role.
Conclusions:
- Nt-acetylation is a fundamental regulatory mechanism with broad biological implications.
- Understanding NATs and Nt-acetylation is crucial for comprehending protein homeostasis and function.
- Further research into NATs' functions and Nt-acetylation mechanisms is warranted.
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