Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

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

EDITORS' CHOICE

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).


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882