Tissue-specific sequence and structural environments of lysine acetylation sites.

摘要: Lysine acetylation is a widespread reversible post-translational modification that regulates broad spectrum of biological activities across various cellular compartments, cell types, tissues, and disease states. While compartment-specific trends in lysine have recently been investigated, its tissue-specific preferences remain unexplored. Here we present comprehensive tissue-based analysis sequence structural features sites (LASs) based on the recent experimental data Lundby et al. (2012). We show acetylated substrates are characterized by motifs both linear amino acid spatial environments. further demonstrate general tendency LASs to reside ordered regions and, specifically, α-helices, also subject tissue specific variation. In line with previous findings generally more evolutionarily conserved than non-LASs, especially proteins known function structurally regular regions. On other hand, as revealed metabolic pathway analysis, diverse functions different tissues frequently associated protein domains. These may imply existence acetyltransferases (KATs) deacetylases (KDACs).