@misc{10481/95397,
year = {2024},
month = {7},
url = {https://hdl.handle.net/10481/95397},
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.},
organization = {Spanish Ministry for Science, Innovation
and Universities/Agencia Estatal de Investigación https://doi.org/10.
13039/501100011033 (grants PID2020-112612GB-I00 to T.K., PID2019-
103972GA-I00 to M.A.M. and PID2020-116261GB-I00 to J.A.G.)},
organization = {Junta
de Andalucía (grant P18-FR-1621 to T.K.)},
organization = {CSIC (grant 2023AEP002 to
M.A.M.)},
organization = {NIH (grant 1R35GM131760 to I.B.Z.)},
publisher = {Nature Research},
title = {Ubiquitous purine sensor modulates diverse signal transduction pathways in bacteria},
doi = {10.1038/s41467-024-50275-3},
author = {Monteagudo Cascales, Elizabet and M. Gumerov, Vadim and Fernández Rodríguez, Matilde and Matilla, Miguel A. and Gavira, Jose A. and B. Zhulin, Igor and Krell, Tino},
}