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Tissue-specific sequence and structural environments of lysine acetylation sites.
J. Struct. Biol. 191, 39-48 (2015)
Lysine acetylation is a widespread reversible post-translational modification that regulates a broad spectrum of biological activities across various cellular compartments, cell types, tissues, and disease states. While compartment-specific trends in lysine acetylation have recently been investigated, its tissue-specific preferences remain unexplored. Here we present a comprehensive tissue-based analysis of sequence and structural features of lysine acetylation sites (LASs) based on the recent experimental data of Lundby et al. (2012). We show that acetylated substrates are characterized by tissue-specific motifs both in linear amino acid sequence and in spatial environments. We further demonstrate that the general tendency of LASs to reside in ordered regions and, specifically, in α-helices, is also subject to tissue specific variation. In line with previous findings we show that LASs are generally more evolutionarily conserved than non-LASs, especially in proteins with known function and in structurally regular regions. On the other hand, as revealed by metabolic pathway analysis, LASs have diverse cellular functions in different tissues and are frequently associated with tissue-specific protein domains. These findings may imply the existence of tissue-specific lysine acetyltranferases (KATs) and lysine deacetylases (KDACs).
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Evolution ; Posttranslational Modifications ; Protein Structure ; Sequence Analysis; Proteome-wide Analysis; Histone Acetyltransferase; Phosphorylation Sites; Proteins; Prediction; Substrate; Database; Reveals; Motifs; Representation
ISSN (print) / ISBN
1047-8477
e-ISSN
1047-8477
Journal
Journal of Structural Biology
Quellenangaben
Volume: 191,
Issue: 1,
Pages: 39-48
Publisher
Elsevier
Publishing Place
San Diego
Non-patent literature
Publications
Reviewing status
Peer reviewed