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Composition and function of the eukaryotic N-terminal acetyltransferase subunits
Bogdan Polevoda1, Fred Sherman
1Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA. Bogdan_Polevoda@urmc.rochester.edu
Biochemical and Biophysical Research Communications
|August 2, 2003
Summary
This study compares N-terminal acetyltransferases (NATs) in yeast and higher eukaryotes, revealing conserved systems but also potential functional differences in subunits. Further research is needed to identify vertebrate NATs and explore yeast NAT functions.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Saccharomyces cerevisiae possesses three N-terminal acetyltransferase (NAT) complexes: NatA, NatB, and NatC.
- These complexes are crucial for protein N-terminal acetylation, a process conserved across eukaryotes.
Purpose of the Study:
- To compare the N-terminal acetylation systems in yeast and higher eukaryotes.
- To investigate potential divergent functions of NAT subunits and their orthologs in vertebrates.
Main Methods:
- Comparative analysis of N-terminally acetylated proteins and NAT orthologous genes.
- Examination of differential expression patterns of NAT subunits.
Main Results:
- Yeast and higher eukaryotes share similar N-terminal acetylation systems.
- Certain NAT subunits show differential expression during development and in carcinomas, suggesting roles in rapid protein synthesis.
- Functional studies of human and mouse NAT orthologs indicate potential non-NAT roles or functional non-equivalence.
Conclusions:
- Vertebrate NAT complexes require definitive identification.
- The non-enzymatic functions of yeast NAT subunits and their orthologs warrant further investigation.
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