Bacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain.

Bacillus subtilis two-component system DegS/U is well known for the complexity of its regulation. The cytosolic sensory kinase DegS does not receive a single predominant input signal like most two-component kinases, instead it integrates a wide array of metabolic inputs that modulate its activity. T...

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Autores principales: Carsten Jers, Ahasanul Kobir, Elsebeth Oline Søndergaard, Peter Ruhdal Jensen, Ivan Mijakovic
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Publicado: Public Library of Science (PLoS) 2011
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Acceso en línea:https://doaj.org/article/716e4e6917ea4a88b553662b39aec58e
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spelling oai:doaj.org-article:716e4e6917ea4a88b553662b39aec58e2021-11-18T06:59:15ZBacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain.1932-620310.1371/journal.pone.0014653https://doaj.org/article/716e4e6917ea4a88b553662b39aec58e2011-02-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21304896/?tool=EBIhttps://doaj.org/toc/1932-6203Bacillus subtilis two-component system DegS/U is well known for the complexity of its regulation. The cytosolic sensory kinase DegS does not receive a single predominant input signal like most two-component kinases, instead it integrates a wide array of metabolic inputs that modulate its activity. The phosphorylation state of the response regulator DegU also does not confer a straightforward "on/off" response; it is fine-tuned and at different levels triggers different sub-regulons. Here we describe serine phosphorylation of the DegS sensing domain, which stimulates its kinase activity. We demonstrate that DegS phosphorylation can be carried out by at least two B. subtilis Hanks-type kinases in vitro, and this stimulates the phosphate transfer towards DegU. The consequences of this process were studied in vivo, using phosphomimetic (Ser76Asp) and non-phosphorylatable (Ser76Ala) mutants of DegS. In a number of physiological assays focused on different processes regulated by DegU, DegS S76D phosphomimetic mutant behaved like a strain with intermediate levels of DegU phosphorylation, whereas DegS S76A behaved like a strain with lower levels of DegU phophorylation. These findings suggest a link between DegS phosphorylation at serine 76 and the level of DegU phosphorylation, establishing this post-translational modification as an additional trigger for this two-component system.Carsten JersAhasanul KobirElsebeth Oline SøndergaardPeter Ruhdal JensenIvan MijakovicPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 2, p e14653 (2011)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Carsten Jers
Ahasanul Kobir
Elsebeth Oline Søndergaard
Peter Ruhdal Jensen
Ivan Mijakovic
Bacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain.
description Bacillus subtilis two-component system DegS/U is well known for the complexity of its regulation. The cytosolic sensory kinase DegS does not receive a single predominant input signal like most two-component kinases, instead it integrates a wide array of metabolic inputs that modulate its activity. The phosphorylation state of the response regulator DegU also does not confer a straightforward "on/off" response; it is fine-tuned and at different levels triggers different sub-regulons. Here we describe serine phosphorylation of the DegS sensing domain, which stimulates its kinase activity. We demonstrate that DegS phosphorylation can be carried out by at least two B. subtilis Hanks-type kinases in vitro, and this stimulates the phosphate transfer towards DegU. The consequences of this process were studied in vivo, using phosphomimetic (Ser76Asp) and non-phosphorylatable (Ser76Ala) mutants of DegS. In a number of physiological assays focused on different processes regulated by DegU, DegS S76D phosphomimetic mutant behaved like a strain with intermediate levels of DegU phosphorylation, whereas DegS S76A behaved like a strain with lower levels of DegU phophorylation. These findings suggest a link between DegS phosphorylation at serine 76 and the level of DegU phosphorylation, establishing this post-translational modification as an additional trigger for this two-component system.
format article
author Carsten Jers
Ahasanul Kobir
Elsebeth Oline Søndergaard
Peter Ruhdal Jensen
Ivan Mijakovic
author_facet Carsten Jers
Ahasanul Kobir
Elsebeth Oline Søndergaard
Peter Ruhdal Jensen
Ivan Mijakovic
author_sort Carsten Jers
title Bacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain.
title_short Bacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain.
title_full Bacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain.
title_fullStr Bacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain.
title_full_unstemmed Bacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain.
title_sort bacillus subtilis two-component system sensory kinase degs is regulated by serine phosphorylation in its input domain.
publisher Public Library of Science (PLoS)
publishDate 2011
url https://doaj.org/article/716e4e6917ea4a88b553662b39aec58e
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