title: Global analysis of lysine acetylation suggests the involvement of protein acetylation in diverse biological processes in rice (Oryza sativa).
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Mississippi State University, Starkville, Mississippi, United States of America.
authors.forename: Babi Ramesh Reddy
authors.initials: BR
authors.lastname: Nallamilli
authors.affiliation: Institute of Genomics, Biocomputing and Biotechnology, Mississippi Agricultural and Forestry Experimental Station, Mississippi State University, Starkville, Mississippi, United States of America.
authors.forename: Mariola J
authors.initials: MJ
authors.lastname: Edelmann
authors.affiliation: Department of Biochemistry and Molecular Biology, Mississippi State University, Starkville, Mississippi, United States of America.
authors.forename: Xiaoxian
authors.initials: X
authors.lastname: Zhong
authors.affiliation: Department of Biochemistry and Molecular Biology, Mississippi State University, Starkville, Mississippi, United States of America.
authors.forename: Feng
authors.initials: F
authors.lastname: Tan
authors.affiliation: Department of Biochemistry and Molecular Biology, Mississippi State University, Starkville, Mississippi, United States of America.
authors.forename: Hana
authors.initials: H
authors.lastname: Mujahid
authors.affiliation: Department of Biochemistry and Molecular Biology, Mississippi State University, Starkville, Mississippi, United States of America.
authors.forename: Jian
authors.initials: J
authors.lastname: Zhang
authors.affiliation: Institute of Genomics, Biocomputing and Biotechnology, Mississippi Agricultural and Forestry Experimental Station, Mississippi State University, Starkville, Mississippi, United States of America ; College of Veterinary Medicine, Mississippi State University, Starkville, Mississippi, United States of America.
authors.forename: Bindu
authors.initials: B
authors.lastname: Nanduri
authors.affiliation: Department of Biochemistry and Molecular Biology, Mississippi State University, Starkville, Mississippi, United States of America.
authors.forename: Zhaohua
authors.initials: Z
authors.lastname: Peng
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D001686:Biological Phenomena; D015153:Blotting, Western; D002846:Chromatography, Affinity; D063990:Gene Ontology; D006801:Humans; D008239:Lysine / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D012275:Oryza; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000032:analysis*; D040901:Proteomics; D053719:Tandem Mass Spectrometry
chemical_list: D010940:Plant Proteins; D020543:Proteome; D008239:Lysine