生物
赖氨酸
乙酰化
黑腹果蝇
磷酸化
保守序列
苏氨酸
生物化学
丝氨酸
蛋白质组
组蛋白
蛋白质组学
细胞生物学
翻译后修饰
乙酰转移酶
化学
计算生物学
基因
肽序列
氨基酸
作者
Brian T. Weinert,Sebastian Wagner,Heiko Horn,Peter Henriksen,Wenshe R. Liu,Jesper V. Olsen,Lars Juhl Jensen,Chunaram Choudhary
出处
期刊:Science Signaling
[American Association for the Advancement of Science (AAAS)]
日期:2011-07-26
卷期号:4 (183)
被引量:226
标识
DOI:10.1126/scisignal.2001902
摘要
Posttranslational modification of proteins by acetylation and phosphorylation regulates most cellular processes in living organisms. Surprisingly, the evolutionary conservation of phosphorylated serine and threonine residues is only marginally higher than that of unmodified serines and threonines. With high-resolution mass spectrometry, we identified 1981 lysine acetylation sites in the proteome of Drosophila melanogaster. We used data sets of experimentally identified acetylation and phosphorylation sites in Drosophila and humans to analyze the evolutionary conservation of these modification sites between flies and humans. Site-level conservation analysis revealed that acetylation sites are highly conserved, significantly more so than phosphorylation sites. Furthermore, comparison of lysine conservation in Drosophila and humans with that in nematodes and zebrafish revealed that acetylated lysines were significantly more conserved than were nonacetylated lysines. Bioinformatics analysis using Gene Ontology terms suggested that the proteins with conserved acetylation control cellular processes such as protein translation, protein folding, DNA packaging, and mitochondrial metabolism. We found that acetylation of ubiquitin-conjugating E2 enzymes was evolutionarily conserved, and mutation of a conserved acetylation site impaired the function of the human E2 enzyme UBE2D3. This systems-level analysis of comparative posttranslational modification showed that acetylation is an anciently conserved modification and suggests that phosphorylation sites may have evolved faster than acetylation sites.
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