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Updated: May 20, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
Interfacing protein lysine acetylation and protein phosphorylation: ancient modifications meet on ancient proteins
Hue T Tran1, R Glen Uhrig, Mhairi Nimick
1University of Calgary, Department of Biological Sciences, Calgary, AB Canada.
Abstract:
Recognition that different protein covalent modifications can operate in concert to regulate a single protein has forced us to re-think the relationship between amino acid side chain modifications and protein function. Results presented by Tran et al. 2012 demonstrate the association of a protein phosphatase (PP2A) with a histone/lysine deacetylase (HDA14) on plant microtubules along with a histone/lysine acetyltransferase (ELP3). This finding reveals a regulatory interface between two prevalent covalent protein modifications, protein phosphorylation and acetylation, emphasizing the integrated complexity of post-translational protein regulation found in nature.
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