Extensive regulation of enzyme activity by phosphorylation in Escherichia coli

While phosphorylation is an essential post-translational modification in eukaryotes only recently the phosphoproteome of prokaryotes has been provided. Here, Schastnaya et al. mutate 52 phosphosites on 23 E. coli enzymes and apply metabolomics to provide evidence for the functional relevance of bact...

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Autores principales:	Evgeniya Schastnaya, Zrinka Raguz Nakic, Christoph H. Gruber, Peter Francis Doubleday, Aarti Krishnan, Nathan I. Johns, Jimin Park, Harris H. Wang, Uwe Sauer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2160c240cd0443caaf59b15567610f60
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spelling	oai:doaj.org-article:2160c240cd0443caaf59b15567610f602021-12-02T17:27:12ZExtensive regulation of enzyme activity by phosphorylation in Escherichia coli10.1038/s41467-021-25988-42041-1723https://doaj.org/article/2160c240cd0443caaf59b15567610f602021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25988-4https://doaj.org/toc/2041-1723While phosphorylation is an essential post-translational modification in eukaryotes only recently the phosphoproteome of prokaryotes has been provided. Here, Schastnaya et al. mutate 52 phosphosites on 23 E. coli enzymes and apply metabolomics to provide evidence for the functional relevance of bacterial phosphorylation events.Evgeniya SchastnayaZrinka Raguz NakicChristoph H. GruberPeter Francis DoubledayAarti KrishnanNathan I. JohnsJimin ParkHarris H. WangUwe SauerNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Evgeniya Schastnaya Zrinka Raguz Nakic Christoph H. Gruber Peter Francis Doubleday Aarti Krishnan Nathan I. Johns Jimin Park Harris H. Wang Uwe Sauer Extensive regulation of enzyme activity by phosphorylation in Escherichia coli
description	While phosphorylation is an essential post-translational modification in eukaryotes only recently the phosphoproteome of prokaryotes has been provided. Here, Schastnaya et al. mutate 52 phosphosites on 23 E. coli enzymes and apply metabolomics to provide evidence for the functional relevance of bacterial phosphorylation events.
format	article
author	Evgeniya Schastnaya Zrinka Raguz Nakic Christoph H. Gruber Peter Francis Doubleday Aarti Krishnan Nathan I. Johns Jimin Park Harris H. Wang Uwe Sauer
author_facet	Evgeniya Schastnaya Zrinka Raguz Nakic Christoph H. Gruber Peter Francis Doubleday Aarti Krishnan Nathan I. Johns Jimin Park Harris H. Wang Uwe Sauer
author_sort	Evgeniya Schastnaya
title	Extensive regulation of enzyme activity by phosphorylation in Escherichia coli
title_short	Extensive regulation of enzyme activity by phosphorylation in Escherichia coli
title_full	Extensive regulation of enzyme activity by phosphorylation in Escherichia coli
title_fullStr	Extensive regulation of enzyme activity by phosphorylation in Escherichia coli
title_full_unstemmed	Extensive regulation of enzyme activity by phosphorylation in Escherichia coli
title_sort	extensive regulation of enzyme activity by phosphorylation in escherichia coli
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/2160c240cd0443caaf59b15567610f60
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Extensive regulation of enzyme activity by phosphorylation in Escherichia coli

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