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Sci. Signal., 26 July 2011
Vol. 4, Issue 183, p. ra48
[DOI: 10.1126/scisignal.2001902]


Editor's Summary

Age of the Acetylome
Acetylation and phosphorylation are regulatory posttranslational modifications that occur on proteins. With proteome-wide data in divergent species, insights regarding the evolution of these two regulatory processes can be revealed. Weinert et al. report the proteome-wide analysis of acetylated proteins in the fruit fly. Comparing the data on acetylated proteins in humans and flies with proteome sequences of nematodes and zebrafish indicated that acetylated sites were more conserved than were nonacetylated sites, and comparison of the human and fly acetylomes with their phosphoproteomes indicated that acetylation sites were more conserved than were phosphorylation sites. Acetylation intersected with another posttranslational modification, ubiquitylation: Acetylation occurred on one-third of human ubiquitin-conjugating E2 enzymes and influenced the activity of these enzymes, suggesting that acetylation provides another regulatory layer for this other type of posttranslational modification.

Citation: B. T. Weinert, S. A. Wagner, H. Horn, P. Henriksen, W. R. Liu, J. V. Olsen, L. J. Jensen, C. Choudhary, Proteome-Wide Mapping of the Drosophila Acetylome Demonstrates a High Degree of Conservation of Lysine Acetylation. Sci. Signal. 4, ra48 (2011).

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