Nα-terminal Acetylation of Eukaryotic Proteins*

By B. Polevoda, F. Sherman. Journal of Biological Chemistry, 2000

333 citations recorded by the source corpus.

The two cotranslational processes, cleavage of N-terminal methionine residues and N-terminal acetylation, are by far the most common modifications, occurring on the vast majority of eukaryotic proteins. Studies with the yeast Saccharomyces cerevisiae revealed three N-terminal acetyltransferases, NatA, NatB, and NatC, that acted on groups of substrates, each containing degenerate motifs. Orthologous genes encoding the three N-terminal acetyltransferases and the patterns of N-terminal acetylation suggest that eukaryotes generally use the same systems for N-terminal acetylation. The biological significance of this N-terminal modification varies with the particular protein, with some proteins requiring acetylation for function, whereas others do not.

Subfields: Molecular Biology, Oncology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/e2af4eddc30bc8adc02f69e660da2e4e0b4032ed

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In Molecular Biology

1. F. Sherman
2. B. Polevoda
3. S. Brown

In Oncology

1. F. Sherman
2. B. Polevoda

Citations in the corpus

• Yeast Nα‐terminal acetyltransferases are associated with ribosomes (2008, methodology): “E-mail: Fred_Sherman@urmc.rochester.edu Received 22 August 2006; Accepted 19 April 2007 DOI 10.1002/jcb.21418 Each NAT is required for acetylating different groups of proteins [Polevoda and Sherman, 2000] (Table I).”