Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation
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Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. / Weinert, Brian T; Wagner, Sebastian A; Horn, Heiko; Henriksen, Peter; Liu, Wenshe R; Olsen, Jesper V; Jensen, Lars J; Choudhary, Chuna Ram.
In: Science Signaling, Vol. 4, No. 183, 2011, p. ra48.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation
AU - Weinert, Brian T
AU - Wagner, Sebastian A
AU - Horn, Heiko
AU - Henriksen, Peter
AU - Liu, Wenshe R
AU - Olsen, Jesper V
AU - Jensen, Lars J
AU - Choudhary, Chuna Ram
PY - 2011
Y1 - 2011
N2 - 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.
AB - 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.
KW - Acetylation
KW - Animals
KW - Computational Biology
KW - DNA Primers
KW - Drosophila Proteins
KW - Drosophila melanogaster
KW - Humans
KW - Lysine
KW - Mass Spectrometry
KW - Phosphorylation
KW - Protein Processing, Post-Translational
KW - Proteomics
KW - Species Specificity
KW - Yeasts
U2 - 10.1126/scisignal.2001902
DO - 10.1126/scisignal.2001902
M3 - Journal article
C2 - 21791702
VL - 4
SP - ra48
JO - Science Signaling
JF - Science Signaling
SN - 1945-0877
IS - 183
ER -
ID: 40289934