Abstract
A second enzyme that removes acetyl groups from lysine residues in E. coli been discovered and represents the founding member of a new enzyme family.
Highlights
The addition of acetyl groups to lysine residues in proteins is an important step in a wide range of biological processes, including the regulation of gene expression, protein-protein interactions and protein stability (Beltrao et al, 2013; Zhang et al, 2009; Glozak et al, 2005; Kouzarides, 2000)
The only lysine deacetylase to have been identified in the bacterium Escherichia coli to date is called CobB, and it belongs to the family of enzymes that rely on a chemical called NAD+ as a cofactor (AbouElfetouh, et al, 2015)
The three potential substrates were proteins that are acetylated heavily in E. coli cells, but are not deacetylated by CobB. They found that an E. coli protein called YcgC was a lysine deacetylase that has RutR – a protein that regulates transcription in E. coli – as a substrate
Summary
The removal of these acetyl groups by enzymes called lysine deacetylases is important (Downey and Baetz, 2015). The only lysine deacetylase to have been identified in the bacterium Escherichia coli to date is called CobB, and it belongs to the family of enzymes that rely on a chemical called NAD+ as a cofactor (AbouElfetouh, et al, 2015). In eLife, a team of researchers from China, Taiwan and the United States – including Shen Tu, ShuJuan Guo and Chien-Sheng Chen as joint first authors – report that they have used a technique called “clip-chip” to identify a new lysine deacetylase in E. coli (Tu et al, 2015).
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