ArticlePloS one2013
C-di-GMP hydrolysis by Pseudomonas aeruginosa HD-GYP phosphodiesterases: analysis of the reaction mechanism and novel roles for pGpG.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 64 citations in OpenAlex.
- STING agonist profiling by nucleotide library defines structural determinants of cyclic dinucleotide recognition.iScience · 2026Article
- Roles of divalent metals in the regulation of cyclic di-GMP signaling in bacteria.Journal of bacteriology · 2026Review
- Structural analyses uncover protease-adhesin interactions and c-di-GMP receptor regulation in sulfate-reducing bacteria.Nature communications · 2026Article
- Defining the role ofJournal of bacteriology · 2026Article
- Virulence Regulation and Lifestyle Transitions: The Role of c-di-GMP and Two-Component Systems in Erwinia amylovora and Their Evolutionary Context Within Enterobacterales.Molecular plant pathology · 2026Review
- Discovery of Novel c-di-GMP-Related Genes inPathogens (Basel, Switzerland) · 2026Article
- Transcriptional profiling ofFrontiers in microbiology · 2026Article
- Environmental purines decrease Pseudomonas aeruginosa biofilm formation by disrupting c-di-GMP metabolism.Cell reports · 2024Article
- CdgB Regulates Morphological Differentiation and Toyocamycin Production inInternational journal of molecular sciences · 2024Article
- A Library of Promoter-Applied and environmental microbiology · 2023Article
- Article
- Sequence Conservation, Domain Architectures, and Phylogenetic Distribution of the HD-GYP Type c-di-GMP Phosphodiesterases.Journal of bacteriology · 2022Review
- Pseudomonas aeruginosa Oligoribonuclease Controls Tolerance to Polymyxin B by Regulating Pel Exopolysaccharide Production.Antimicrobial agents and chemotherapy · 2022Article
- Sensory Perception in Bacterial Cyclic Diguanylate Signal Transduction.Journal of bacteriology · 2022Review
- Nitric oxide-secreting probiotics as sustainable bio-cleaners for reverse osmosis membrane systems.Environmental science and pollution research international · 2022Review
- Genome characterization of a uropathogenicFrontiers in cellular and infection microbiology · 2022Article
- Phenotypic and integrated analysis of a comprehensiveFrontiers in microbiology · 2022Article
- Article
- Studying GGDEF Domain in the Act: Minimize Conformational Frustration to Prevent Artefacts.Life (Basel, Switzerland) · 2021Article
- Putative Nucleotide-Based Second Messengers in the Archaeal Model OrganismsFrontiers in microbiology · 2021Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In biofilms, the bacterial community optimizes the strategies to sense the environment and to communicate from cell to cell. A key player in the development of a bacterial biofilm is the second messenger c-di-GMP, whose intracellular levels are modulated by the opposite activity of diguanylate cyclases and phosphodiesterases. Given the huge impact of bacterial biofilms on human health, understanding the molecular details of c-di-GMP metabolism represents a critical step in the development of novel therapeutic approaches against biofilms. In this study, we present a detailed biochemical characterization of two c-di-GMP phosphodiesterases of the HD-GYP subtype from the human pathogen Pseudomonas aeruginosa, namely PA4781 and PA4108. Upstream of the catalytic HD-GYP domain, PA4781 contains a REC domain typical of two-component systems, while PA4108 contains an uncharacterized domain of unknown function. Our findings shed light on the activity and catalytic mechanism of these phosphodiesterases. We show that both enzymes hydrolyse c-di-GMP in a two-step reaction via the linear intermediate pGpG and that they produce GMP in vitro at a surprisingly low rate. In addition, our data indicate that the non-phosphorylated REC domain of PA4781 prevents accessibility of c-di-GMP to the active site. Both PA4108 and phosphorylated PA4781 are also capable to use pGpG as an alternative substrate and to hydrolyse it into GMP; the affinity of PA4781 for pGpG is one order of magnitude higher than that for c-di-GMP. These results suggest that these enzymes may not work (primarily) as genuine phosphodiesterases. Moreover, the unexpected affinity of PA4781 for pGpG may indicate that pGpG could also act as a signal molecule in its own right, thus further widening the c-di-GMP-related signalling scenario.
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