Susan M. Hancock

TL;DR: It is revealed that lysine acetylation is a prevalent modification in enzymes that catalyze intermediate metabolism, and plays a major role in metabolic regulation.

TL;DR: This work reports a general method for the production of homogeneously and site-specifically acetylated recombinant histones by genetically encoding acetyl-lysine and demonstrates that, in contrast to the prevailing dogma, acetylation of H3 K56 does not directly affect the compaction of chromatin and has modest effects on remodeling by SWI/SNF and RSC.

TL;DR: The discovery of a simple system through which variant pyrrolysyl-tRNA synthetase/tRNACUAPyl pairs created in Escherichia coli can be used to expand the genetic code of Saccharomyces cerevisiae is reported.

TL;DR: This work evolves an orthogonal aminoacyl-tRNA synthetase/tRNACUA pair that directs the efficient incorporation of phosphoserine (pSer (1)) into recombinant proteins in Escherichia coli, and purify proteins bearing biologically relevant phosphorylations that were previously challenging or impossible to access.

TL;DR: The evolution of the PylRS/tRNACUA pair for genetically encoding photocaged cysteine is demonstrated and the utility of this approach is demonstrated by rapidly activating TEV protease following illumination of single cells.