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 The worth of creating in depth, tissue-particular maps of protein lysine acetylation websites is further underscored by the numerous function of posttranslational modifications in the evolution and phenotypic composition of vertebrates, as indicated by the significant selective pressure gene regulatory parts near posttranslational-modifying enzymes have come underneath in placental animals ( Lowe et al., 2011 ). Here, we mixed an environment friendly technique for protein extraction from tissue samples with lysine-acetylated peptide immunoprecipitation and excessive-accuracy tandem mass spectrometric (MS/MS) measurements, which allowed us to generate an atlas of lysine acetylation websites in 16 completely different rat tissues.
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