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Access through your institution Buy or subscribe Post-translational modifications, such as protein acetylation, are important for the regulation of protein function. Protein acetylation is
widespread in _Escherichia coli_, but so far only one deacetylase, CobB, has been identified. To find new deacetylases, Tu, Guo and Chen _et al_. developed a 'clip-chip' assay, in
which proteins with potential enzymatic activity are arrayed on a glass slide and clipped to a slide with substrate. The serine hydrolase YcgC mediated the loss of acetylation of several
substrates, which were distinct from those substrates targeted by CobB. YcgC homologues have been found in other bacteria and a selection of these homologues were tested _in vivo_,
confirming their deacetylase activity. Thus, YcgC and its homologues represent a new family of deacetylases in bacteria and a new type of deacetylase as none of the previously identified
enzymes are serine hydrolases. This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your institution Subscribe to this journal Receive 12
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REFERENCES * Tu, S., Guo, S. J., Chen, C. S. et al. YcgC represents a new protein deacetylase family in prokaryotes. _eLife_ 4, e05322 (2015) Article Google Scholar Download references
Authors * Ursula Hofer View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS
ARTICLE Hofer, U. A novel family of bacterial protein deacetylases. _Nat Rev Microbiol_ 14, 65 (2016). https://doi.org/10.1038/nrmicro.2016.6 Download citation * Published: 19 January 2016 *
Issue Date: February 2016 * DOI: https://doi.org/10.1038/nrmicro.2016.6 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content: Get shareable link
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