A c-di-GMP signaling module controls responses to iron in Pseudomonas aeruginosa

Xueliang Zhan, Kuo Zhang, Chenchen Wang, Qiao Fan, Xiujia Tang, Xi Zhang, Ke Wang, Yang Fu and Haihua Liang ()
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Xueliang Zhan: Northwest University
Kuo Zhang: Southern University of Science and Technology
Chenchen Wang: Southern University of Science and Technology
Qiao Fan: Northwest University
Xiujia Tang: The First Affiliated Hospital of Guangxi Medical University
Xi Zhang: Northwest University
Ke Wang: The First Affiliated Hospital of Guangxi Medical University
Yang Fu: Southern University of Science and Technology
Haihua Liang: Southern University of Science and Technology

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

Abstract: Abstract Cyclic dimeric guanosine monophosphate (c-di-GMP) serves as a bacterial second messenger that modulates various processes including biofilm formation, motility, and host-microbe symbiosis. Numerous studies have conducted comprehensive analysis of c-di-GMP. However, the mechanisms by which certain environmental signals such as iron control intracellular c-di-GMP levels are unclear. Here, we show that iron regulates c-di-GMP levels in Pseudomonas aeruginosa by modulating the interaction between an iron-sensing protein, IsmP, and a diguanylate cyclase, ImcA. Binding of iron to the CHASE4 domain of IsmP inhibits the IsmP-ImcA interaction, which leads to increased c-di-GMP synthesis by ImcA, thus promoting biofilm formation and reducing bacterial motility. Structural characterization of the apo-CHASE4 domain and its binding to iron allows us to pinpoint residues defining its specificity. In addition, the cryo-electron microscopy structure of ImcA in complex with a c-di-GMP analog (GMPCPP) suggests a unique conformation in which the compound binds to the catalytic pockets and to the membrane-proximal side located at the cytoplasm. Thus, our results indicate that a CHASE4 domain directly senses iron and modulates the crosstalk between c-di-GMP metabolic enzymes.

Date: 2024
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DOI: 10.1038/s41467-024-46149-3

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