Ubiquitous purine sensor modulates diverse signal transduction pathways in bacteria

Elizabet Monteagudo-Cascales, Vadim M. Gumerov, Matilde Fernández, Miguel A. Matilla, José A. Gavira, Igor B. Zhulin () and Tino Krell ()
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Elizabet Monteagudo-Cascales: Consejo Superior de Investigaciones Científicas
Vadim M. Gumerov: The Ohio State University
Matilde Fernández: Universidad de Granada
Miguel A. Matilla: Consejo Superior de Investigaciones Científicas
José A. Gavira: Laboratory of Crystallographic Studies (CSIC-UGR)
Igor B. Zhulin: The Ohio State University
Tino Krell: Consejo Superior de Investigaciones Científicas

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract 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.

Date: 2024
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-50275-3

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DOI: 10.1038/s41467-024-50275-3

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