CELLULAR JOY STICK
SARAH EVERTS · Chemical & Engineering News · 2010
SCIENTISTS HAVE KNOWN for decades that proteins can be acetylated on their lysine residues, but the modification was long seen as the poor cousin to phosphorylation, which can activate or deactivate countless processes in living cells. New research, however, reveals that acetylation is a master switch for a who’s who of cellular functions in organisms as diverse as bacteria and humans. The widespread acetylation of important proteins will likely inspire drugmakers to target enzymes that can decorate or undress proteins with acetyl groups. Acetylation is probably best known for its role in controlling which genes in a cell are put into deep storage and which ones can be accessed by transcription machinery. Hints of its versatility came last year, when researchers including Chunaram Choudhary, a biochemist at the University of Copenhagen, found that thousands of additional proteins are acetylated, including some involved in cell division and DNA repair. Now, a team including Guo-Ping Zhao ...