College of Agriculture & Life Sciences Publications and Scholarship


Lysine acetylation is a reversible, dynamic protein modification regulated by lysine acetyltransferases and deacetylases. Recent advances in high-throughput proteomics have greatly contributed to the success of global analysis of lysine acetylation. A large number of proteins of diverse biological functions have been shown to be acetylated in several reports in human cells, E.coli, and dicot plants. However, the extent of lysine acetylation in non-histone proteins remains largely unknown in monocots, particularly in the cereal crops. Here we report the mass spectrometric examination of lysine acetylation in rice (Oryza sativa). We identified 60 lysine acetylated sites on 44 proteins of diverse biological functions. Immunoblot studies further validated the presence of a large number of acetylated non-histone proteins. Examination of the amino acid composition revealed substantial amino acid bias around the acetylation sites and the amino acid preference is conserved among different organisms. Gene ontology analysis demonstrates that lysine acetylation occurs in diverse cytoplasmic, chloroplast and mitochondrial proteins in addition to the histone modifications. Our results suggest that lysine acetylation might constitute a regulatory mechanism for many proteins, including both histones and non-histone proteins of diverse biological functions.


Public Library of Science

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College of Agriculture and Life Sciences


Department of Biochemistry and Molecular Biology


Acetylation, Affinity, Amino Acid Sequence, Biological Processes, Blotting, Chromatography, Gene Ontology, Humans, Lysine, Lysine: chemistry, Lysine: metabolism, Molecular Sequence Data, Oryza sativa, Plant Proteins, Plant Proteins: genetics, Plant Proteins: metabolism, Post-Translational, Protein Processing, Proteome, Proteome: analysis, Proteomics, Tandem Mass Spectrometry, Western



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Biochemistry Commons