Location: Plant Genetics ResearchTitle: A bioinformatics-based overview of protein Lys-Ne-acetylation Author
|Rao, Shyama - University Of Missouri|
|Thelen, Jay - University Of Missouri|
Submitted to: Frontiers in Plant Science
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 3/18/2014
Publication Date: 7/17/2014
Publication URL: http://handle.nal.usda.gov/10113/59464
Citation: Rao, S.R., Thelen, J.J., Miernyk, J.A. 2014. A bioinformatics-based overview of protein Lys-Ne-acetylation. Frontiers in Plant Science. 5:1-11. Interpretive Summary: We have identified an important chemical modification of plant proteins. This modification has the potential to control the activity and location of the protein being modified, or which other proteins are associated with it. The chemical modification can be reversed. By using data mining and statistical/mathematical analysis the systems essential for alteration and removal of the modification were characterized. Furthermore, we have identified and analyzed a class of proteins that can recognize the chemical modification and bind proteins that have it. This information has the potential to help with a detailed understanding of plant metabolism, growth and development, and reproduction. In terms of crop plants such as soybeans, there is the potential that our understanding of this chemical modification will allow the development of lines with greater yields or custom-designed composition. The information will be most useful to to other scientists, including breeders and those using a biotech-approach to modifying seed composition.
Technical Abstract: Among posttranslational modifications, there are some conceptual similarities between Lys-N'-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; thousands 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 posttranslational modifications of histones, more recent studies have addressed metabolic regulation. Being directly coupled with cellular CoA/acetyl-CoA and NAD/NADH, reversible Lys-N'-acetylation has the potential to control, or contribute to control, of primary metabolism, signaling, and growth and development.