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Updated: Apr 29, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
Is Lys-Nɛ-acetylation the next big thing in post-translational modifications?
R Shyama Prasad Rao1, Jay J Thelen1, Ján A Miernyk2
1Division of Biochemistry, USDA, Agricultural Research Service, University of Missouri, Columbia, MO 65211, USA; Interdisciplinary Plant Group, USDA, Agricultural Research Service, University of Missouri, Columbia, MO 65211, USA.
Abstract:
Lys-N(ɛ)-acetylation (PKA) has recently ascended from a post-translational modification (PTM) of limited distribution to one approaching the abundance of O-phosphorylation. Thousands of KAC proteins have been identified in Archaea, bacteria, and Eukarya, and the KAC system of acetyltransferases, deacetylases, and binding proteins is superficially comparable with the kinases, phosphatases, and phospho- (P-)protein binding-proteins of O-phosphorylation. Herein, we describe recent results and compare several aspects of these two major systems of PTM in plants.
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