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TitleA c-di-GMP signaling module controls responses to iron in Pseudomonas aeruginosa.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 1860, Year 2024
Publish dateFeb 29, 2024
AuthorsXueliang Zhan / Kuo Zhang / Chenchen Wang / Qiao Fan / Xiujia Tang / Xi Zhang / Ke Wang / Yang Fu / Haihua Liang /
PubMed AbstractCyclic 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 ...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.
External linksNat Commun / PubMed:38424057 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.9 - 3.2 Å
Structure data

37444

8wcn

EMDB-37444, PDB-8wcn:
Cryo-EM structure of PAO1-ImcA with GMPCPP
Method: EM (single particle) / Resolution: 3.2 Å

PDB-8wct:
The crystal structure of the CHASE4 domain of iron-sensetive membrane protein (IsmP,Uniprot ID:Q9I243)
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-G2P:
PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-CPP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-HOH:
WATER / Water

Source
  • pseudomonas aeruginosa (bacteria)
KeywordsMEMBRANE PROTEIN / GGDEF domain / diguanylate cyclase activity / CHEASE4 domain / iron-sensetive

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