Ubiquitous purine sensor modulates diverse signal transduction pathways in bacteria.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
12 Jul 2024
12 Jul 2024
Historique:
received:
13
11
2023
accepted:
05
07
2024
medline:
13
7
2024
pubmed:
13
7
2024
entrez:
12
7
2024
Statut:
epublish
Résumé
Purines and their derivatives control intracellular energy homeostasis and nucleotide synthesis, and act as signaling molecules. Here, we combine structural and sequence information to define a purine-binding motif that is present in sensor domains of thousands of bacterial receptors that modulate motility, gene expression, metabolism, and second-messenger turnover. Microcalorimetric titrations of selected sensor domains validate their ability to specifically bind purine derivatives, and evolutionary analyses indicate that purine sensors share a common ancestor with amino-acid receptors. Furthermore, we provide experimental evidence of physiological relevance of purine sensing in a second-messenger signaling system that modulates c-di-GMP levels.
Identifiants
pubmed: 38997289
doi: 10.1038/s41467-024-50275-3
pii: 10.1038/s41467-024-50275-3
doi:
Substances chimiques
Purines
0
Bacterial Proteins
0
Cyclic GMP
H2D2X058MU
bis(3',5')-cyclic diguanylic acid
61093-23-0
purine
W60KTZ3IZY
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
5867Subventions
Organisme : Consejería de Economía, Innovación, Ciencia y Empleo, Junta de Andalucía (Ministry of Economy, Innovation, Science and Employment, Government of Andalucia)
ID : P18-FR-1621
Informations de copyright
© 2024. The Author(s).
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