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In silico analysis of protein Lys-N(𝜀)-acetylation in plants.
- Source :
-
Frontiers in plant science [Front Plant Sci] 2014 Aug 04; Vol. 5, pp. 381. Date of Electronic Publication: 2014 Aug 04 (Print Publication: 2014). - Publication Year :
- 2014
-
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.
Details
- Language :
- English
- ISSN :
- 1664-462X
- Volume :
- 5
- Database :
- MEDLINE
- Journal :
- Frontiers in plant science
- Publication Type :
- Academic Journal
- Accession number :
- 25136347
- Full Text :
- https://doi.org/10.3389/fpls.2014.00381