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Comment on ‘YcgC represents a new protein deacetylase family in prokaryotes’

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 tha...

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Autores principales: Kremer, Magdalena, Kuhlmann, Nora, Lechner, Marius, Baldus, Linda, Lammers, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6023612/
https://www.ncbi.nlm.nih.gov/pubmed/29939131
http://dx.doi.org/10.7554/eLife.37798
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author Kremer, Magdalena
Kuhlmann, Nora
Lechner, Marius
Baldus, Linda
Lammers, Michael
author_facet Kremer, Magdalena
Kuhlmann, Nora
Lechner, Marius
Baldus, Linda
Lammers, Michael
author_sort Kremer, Magdalena
collection PubMed
description 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.
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spelling pubmed-60236122018-07-05 Comment on ‘YcgC represents a new protein deacetylase family in prokaryotes’ Kremer, Magdalena Kuhlmann, Nora Lechner, Marius Baldus, Linda Lammers, Michael eLife Biochemistry and Chemical Biology 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. eLife Sciences Publications, Ltd 2018-06-25 /pmc/articles/PMC6023612/ /pubmed/29939131 http://dx.doi.org/10.7554/eLife.37798 Text en © 2018, Kremer et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Biochemistry and Chemical Biology
Kremer, Magdalena
Kuhlmann, Nora
Lechner, Marius
Baldus, Linda
Lammers, Michael
Comment on ‘YcgC represents a new protein deacetylase family in prokaryotes’
title Comment on ‘YcgC represents a new protein deacetylase family in prokaryotes’
title_full Comment on ‘YcgC represents a new protein deacetylase family in prokaryotes’
title_fullStr Comment on ‘YcgC represents a new protein deacetylase family in prokaryotes’
title_full_unstemmed Comment on ‘YcgC represents a new protein deacetylase family in prokaryotes’
title_short Comment on ‘YcgC represents a new protein deacetylase family in prokaryotes’
title_sort comment on ‘ycgc represents a new protein deacetylase family in prokaryotes’
topic Biochemistry and Chemical Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6023612/
https://www.ncbi.nlm.nih.gov/pubmed/29939131
http://dx.doi.org/10.7554/eLife.37798
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