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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2018
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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. |
format | Online Article Text |
id | pubmed-6023612 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
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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