Plant protein lysine acetylation
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[ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI AT AUTHOR'S REQUEST.] Amongst the hundreds of known protein posttranslational modifications, lysine acetylation is noteworthy for its widespread distribution, and for having been recognized as such only recently. In addition to more comprehensively studied nuclear targets and effects of lysine acetylation, in several cases, various effects of acetylation on enzymatic activities have been described. The modification has now been found to occurring on thousands of proteins from diverse species, yet as recently as 2011 was virtually unheard of in plant species. Presented herein are initial descriptions of the developing soybean seed lysine acetylome, and both the pea seedling mitochondrial proteome and acetylome. A quantitative mass spectrometric assay for lysine acetyltransferase activity is presented, as is a method for compiling an aggregate protein database to enable more comprehensive proteomics of organisms with unsequenced genomes.
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