Comment on "YcgC represents a new protein deacetylase family in prokaryotes"
- University of Cologne, Germany
Abstract
Lysine acetylation is a post-translational modification that is conserved from bacteria to humans. It is catalysed by the activities of lysine acetyltransferases, which use acetyl-CoA as the acetyl-donor molecule, and lysine deacetylases, which remove the acetyl moiety. Recently, it was reported that YcgC represents a new prokaryotic deacetylase family with no apparent homologies to existing deacetylases (Tu et al., 2015). Here we report the results of experiments which demonstrate that YcgC is not a deacetylase.
Data availability
All data generated or analyses during this study are included in the manuscript and supporting files.
Article and author information
Author details
Funding
Deutsche Forschungsgemeinschaft (LA 2984/3-1)
- Michael Lammers
Deutsche Forschungsgemeinschaft (CECAD)
- Magdalena Kremer
- Kuhlmann Nora
- Marius Lechner
- Linda Baldus
- Michael Lammers
Boehringer Ingelheim Fonds (Exploration Grant)
- Kuhlmann Nora
Deutsche Forschungsgemeinschaft (Cologne Graduate School of Ageing Research)
- Magdalena Kremer
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Copyright
© 2018, Kremer et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
Metrics
-
- 1,336
- views
-
- 132
- downloads
-
- 10
- citations
Views, downloads and citations are aggregated across all versions of this paper published by eLife.
Download links
A two-part list of links to download the article, or parts of the article, in various formats.
Downloads (link to download the article as PDF)
Open citations (links to open the citations from this article in various online reference manager services)
Cite this article (links to download the citations from this article in formats compatible with various reference manager tools)
Comment on "YcgC represents a new protein deacetylase family in prokaryotes"
eLife 7:e37798.
https://doi.org/10.7554/eLife.37798
Further reading
-
- Biochemistry and Chemical Biology
- Structural Biology and Molecular Biophysics
Nature has inspired the design of improved inhibitors for cancer-causing proteins.
-
- Biochemistry and Chemical Biology
Mutations in the kinase and juxtamembrane domains of the MET Receptor Tyrosine Kinase are responsible for oncogenesis in various cancers and can drive resistance to MET-directed treatments. Determining the most effective inhibitor for each mutational profile is a major challenge for MET-driven cancer treatment in precision medicine. Here, we used a deep mutational scan (DMS) of ~5764 MET kinase domain variants to profile the growth of each mutation against a panel of 11 inhibitors that are reported to target the MET kinase domain. We validate previously identified resistance mutations, pinpoint common resistance sites across type I, type II, and type I ½ inhibitors, unveil unique resistance and sensitizing mutations for each inhibitor, and verify non-cross-resistant sensitivities for type I and type II inhibitor pairs. We augment a protein language model with biophysical and chemical features to improve the predictive performance for inhibitor-treated datasets. Together, our study demonstrates a pooled experimental pipeline for identifying resistance mutations, provides a reference dictionary for mutations that are sensitized to specific therapies, and offers insights for future drug development.
