title: In silico analysis of protein Lys-N(𝜀)-acetylation in plants.
abstract: Among post-translational modifications, there are some conceptual similarities between Lys-N(𝜀)-acetylation and Ser/Thr/Tyr O-phosphorylation. Herein we present a bioinformatics-based overview of reversible protein Lys-acetylation, including some comparisons with reversible protein phosphorylation. The study of Lys-acetylation of plant proteins has lagged behind studies of mammalian and microbial cells; 1000s of acetylation sites have been identified in mammalian proteins compared with only hundreds of sites in plant proteins. While most previous emphasis was focused on post-translational modifications of histones, more recent studies have addressed metabolic regulation. Being directly coupled with cellular CoA/acetyl-CoA and NAD/NADH, reversible Lys-N(𝜀)-acetylation has the potential to control, or contribute to control, of primary metabolism, signaling, and growth and development.
authors.affiliation: Division of Biochemistry, University of Missouri Columbia, MO, USA ; Interdisciplinary Plant Group, University of Missouri Columbia, MO, USA.
authors.forename: R Shyama Prasad
authors.initials: RS
authors.lastname: Rao
authors.affiliation: Division of Biochemistry, University of Missouri Columbia, MO, USA ; Interdisciplinary Plant Group, University of Missouri Columbia, MO, USA.
authors.forename: Jay J
authors.initials: JJ
authors.lastname: Thelen
authors.affiliation: Division of Biochemistry, University of Missouri Columbia, MO, USA ; Interdisciplinary Plant Group, University of Missouri Columbia, MO, USA ; Plant Genetics Research Unit, United States Department of Agriculture - Agricultural Research Service Columbia, MO, USA.
authors.forename: Ján A
authors.initials: JA
authors.lastname: Miernyk
keywords: acetyltransferase; bromodomain; deacetylase; interactome; post-translational modification; regulation; signaling