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dc.contributor.authorNallamilli, Babi Ramesh Reddy
dc.contributor.authorEdelmann, Mariola J.
dc.contributor.authorZhong, Xiaoxian
dc.contributor.authorTan, Feng
dc.contributor.authorMujahid, Hana
dc.contributor.authorZhang, Jian
dc.contributor.authorNanduri, Bindu
dc.contributor.authorPeng, Zhaohua
dc.date.accessioned2015-10-09T19:50:45Z
dc.date.available2015-10-09T19:50:45Z
dc.date.issued2/20/2014
dc.identifier.issn1932-6203
dc.identifier.urihttp://hdl.handle.net/11668/2489
dc.identifier.urihttp://dx.doi.org/10.1371/journal.pone.0089283
dc.description.abstractLysine 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.
dc.publisherPublic Library of Science
dc.relation.ispartofseriesPLoS ONE (Volume 9, Issue 2)
dc.subject.otherAcetylation
dc.subject.otherAffinity
dc.subject.otherAmino Acid Sequence
dc.subject.otherBiological Processes
dc.subject.otherBlotting
dc.subject.otherChromatography
dc.subject.otherGene Ontology
dc.subject.otherHumans
dc.subject.otherLysine
dc.subject.otherLysine: chemistry
dc.subject.otherLysine: metabolism
dc.subject.otherMolecular Sequence Data
dc.subject.otherOryza sativa
dc.subject.otherPlant Proteins
dc.subject.otherPlant Proteins: genetics
dc.subject.otherPlant Proteins: metabolism
dc.subject.otherPost-Translational
dc.subject.otherProtein Processing
dc.subject.otherProteome
dc.subject.otherProteome: analysis
dc.subject.otherProteomics
dc.subject.otherTandem Mass Spectrometry
dc.subject.otherWestern
dc.titleGlobal analysis of lysine acetylation suggests the involvement of protein acetylation in diverse biological processes in rice (Oryza sativa).
dc.typeArticle
dc.publisher.departmentDepartment of Biochemistry and Molecular Biology
dc.publisher.collegeCollege of Agriculture and Life Sciences
dc.identifier.doi10.1371/journal.pone.0089283
dc.publisher.researchcenterInstitute for Genomics, Biocomputing and Biotechnology


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