Ubiquitous purine sensor modulates diverse signal transduction pathways in bacteria.
Nat Commun
; 15(1): 5867, 2024 Jul 12.
Article
in En
| MEDLINE
| ID: mdl-38997289
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Purines
/
Bacterial Proteins
/
Signal Transduction
Language:
En
Journal:
Nat Commun
Journal subject:
BIOLOGIA
/
CIENCIA
Year:
2024
Document type:
Article
Affiliation country:
Country of publication: