A meet-up of two second messengers: the c-di-AMP receptor DarB controls (p)ppGpp synthesis in Bacillus subtilis

In several bacteria, cyclic di-AMP mediates potassium (K+) and osmotic homeostasis. Here, the authors show that DarB, a Bacillus subtilis protein previously reported to bind cyclic di-AMP, interacts with the (p)ppGpp synthetase/hydrolase Rel in a K+-dependent manner in turn leading to Rel-dependent...

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Autores principales:	Larissa Krüger, Christina Herzberg, Dennis Wicke, Heike Bähre, Jana L. Heidemann, Achim Dickmanns, Kerstin Schmitt, Ralf Ficner, Jörg Stülke
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/09902e6043b6418cada4e487ae632736
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spelling	oai:doaj.org-article:09902e6043b6418cada4e487ae6327362021-12-02T10:59:13ZA meet-up of two second messengers: the c-di-AMP receptor DarB controls (p)ppGpp synthesis in Bacillus subtilis10.1038/s41467-021-21306-02041-1723https://doaj.org/article/09902e6043b6418cada4e487ae6327362021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21306-0https://doaj.org/toc/2041-1723In several bacteria, cyclic di-AMP mediates potassium (K+) and osmotic homeostasis. Here, the authors show that DarB, a Bacillus subtilis protein previously reported to bind cyclic di-AMP, interacts with the (p)ppGpp synthetase/hydrolase Rel in a K+-dependent manner in turn leading to Rel-dependent accumulation of pppGpp under conditions of K+ starvation.Larissa KrügerChristina HerzbergDennis WickeHeike BähreJana L. HeidemannAchim DickmannsKerstin SchmittRalf FicnerJörg StülkeNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Larissa Krüger Christina Herzberg Dennis Wicke Heike Bähre Jana L. Heidemann Achim Dickmanns Kerstin Schmitt Ralf Ficner Jörg Stülke A meet-up of two second messengers: the c-di-AMP receptor DarB controls (p)ppGpp synthesis in Bacillus subtilis
description	In several bacteria, cyclic di-AMP mediates potassium (K+) and osmotic homeostasis. Here, the authors show that DarB, a Bacillus subtilis protein previously reported to bind cyclic di-AMP, interacts with the (p)ppGpp synthetase/hydrolase Rel in a K+-dependent manner in turn leading to Rel-dependent accumulation of pppGpp under conditions of K+ starvation.
format	article
author	Larissa Krüger Christina Herzberg Dennis Wicke Heike Bähre Jana L. Heidemann Achim Dickmanns Kerstin Schmitt Ralf Ficner Jörg Stülke
author_facet	Larissa Krüger Christina Herzberg Dennis Wicke Heike Bähre Jana L. Heidemann Achim Dickmanns Kerstin Schmitt Ralf Ficner Jörg Stülke
author_sort	Larissa Krüger
title	A meet-up of two second messengers: the c-di-AMP receptor DarB controls (p)ppGpp synthesis in Bacillus subtilis
title_short	A meet-up of two second messengers: the c-di-AMP receptor DarB controls (p)ppGpp synthesis in Bacillus subtilis
title_full	A meet-up of two second messengers: the c-di-AMP receptor DarB controls (p)ppGpp synthesis in Bacillus subtilis
title_fullStr	A meet-up of two second messengers: the c-di-AMP receptor DarB controls (p)ppGpp synthesis in Bacillus subtilis
title_full_unstemmed	A meet-up of two second messengers: the c-di-AMP receptor DarB controls (p)ppGpp synthesis in Bacillus subtilis
title_sort	meet-up of two second messengers: the c-di-amp receptor darb controls (p)ppgpp synthesis in bacillus subtilis
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/09902e6043b6418cada4e487ae632736
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A meet-up of two second messengers: the c-di-AMP receptor DarB controls (p)ppGpp synthesis in Bacillus subtilis

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