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Sci. Signal., 8 November 2011
Vol. 4, Issue 198, p. ec315
[DOI: 10.1126/scisignal.4198ec315]


Biochemistry Getting Connected

Stella M. Hurtley

Science, AAAS, Cambridge CB2 1LQ, UK

Acetylation of lysine residues in proteins can mediate protein-protein interactions, although few structural mechanisms of acetylation-dependent protein recognition have been elucidated. A common form of protein acetylation is N-terminal acetylation, which occurs cotranslationally for an estimated 30 to 90% of eukaryotic proteins. It is unclear how an N-terminally acetylated amino acid directly mediates protein-protein interactions. Scott et al. report that N-terminal acetylation of the E2 enzyme, Ubc12, dictates distinctive E3-mediated Nedd8 ligation to cullins. This mechanism of protein regulation connects protein acetylation with posttranslational modification by ubiquitin-like proteins.

D. C. Scott, J. K. Monda, E. J. Bennett, J. W. Harper, B. A. Schulman, N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex. Science 334, 674–678 (2011). [Abstract] [Full Text]

Citation: S. M. Hurtley, Getting Connected. Sci. Signal. 4, ec315 (2011).

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