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Karabulut, N.P.* ; Frishman, D.

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

J. Struct. Biol. 191, 39-48 (2015)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Evolution ; Posttranslational Modifications ; Protein Structure ; Sequence Analysis; Proteome-wide Analysis; Histone Acetyltransferase; Phosphorylation Sites; Proteins; Prediction; Substrate; Database; Reveals; Motifs; Representation
Sprache englisch
Veröffentlichungsjahr 2015
HGF-Berichtsjahr 2015
ISSN (print) / ISBN 1047-8477
e-ISSN 1047-8477
Zeitschrift Journal of Structural Biology
Quellenangaben Band: 191, Heft: 1, Seiten: 39-48 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort San Diego
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Bioinformatics and Systems Biology (IBIS)
POF Topic(s) 30505 - New Technologies for Biomedical Discoveries
Forschungsfeld(er) Enabling and Novel Technologies
PSP-Element(e) G-503700-001
PubMed ID 26049078
DOI 10.1016/j.jsb.2015.06.001
WOS ID WOS:000357907700005
Scopus ID 84937640159
Scopus ID 84930372628
Erfassungsdatum 2015-06-08
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