ArticleThe Journal of biological chemistry2016
Phosphoryl Group Flow within the Pseudomonas aeruginosa Pil-Chp Chemosensory System: DIFFERENTIAL FUNCTION OF THE EIGHT PHOSPHOTRANSFERASE AND THREE RECEIVER DOMAINS.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Distinct roles of PilI and ChpC inApplied and environmental microbiology · 2026Article
- The type IV pilus steering committee: how Pil-Chp controls directional motility.Journal of bacteriology · 2025Review
- FimX regulates type IV pilus localization via the Pil-Chp chemosensory system inMolecular biology of the cell · 2025Article
- Antagonistic response regulators spatially regulate receptor methylation in the Pseudomonas aeruginosa Pil-Chp surface sensing system.Cell reports · 2025Article
- The type IV pilus chemoreceptor PilJ controls chemotaxis of one bacterial species towards another.PLoS biology · 2024Article
- Diverse domain architectures of CheA histidine kinase, a central component of bacterial and archaeal chemosensory systems.Microbiology spectrum · 2024Article
- A cyanobacterial chemotaxis-like system controls phototactic orientation via phosphorylation of two antagonistic response regulators.microLife · 2024Article
- Evidence for the Type IV Pilus Retraction Motor PilT as a Component of the Surface Sensing System in Pseudomonas aeruginosa.Journal of bacteriology · 2023Article
- Evidence for the Type IV Pili Retraction Motor PilT as a Component of the Surface Sensing System inbioRxiv : the preprint server for biology · 2023Article
- Two antagonistic response regulators control Pseudomonas aeruginosa polarization during mechanotaxis.The EMBO journal · 2023Article
- The Cellular Abundance of Chemoreceptors, Chemosensory Signaling Proteins, Sensor Histidine Kinases, and Solute Binding Proteins ofInternational journal of molecular sciences · 2023Article
- Reversible adhesion by type IV pili leads to formation of permanent localized clusters.iScience · 2022Article
- Generalizable strategy to analyze domains in the context of parent protein architecture: A CheW case study.Proteins · 2022Article
- Surface-Induced cAMP Signaling Requires Multiple Features of the Pseudomonas aeruginosa Type IV Pili.Journal of bacteriology · 2022Article
- Pilus Production in Acinetobacter baumannii Is Growth Phase Dependent and Essential for Natural Transformation.Journal of bacteriology · 2021Article
- Review
- Article
- Sigma factor RpoN employs a dual transcriptional regulation for controlling twitching motility and biofilm formation in Lysobacter enzymogenes OH11.Current genetics · 2018Article
- Cyclic AMP-Independent Control of Twitching Motility in Pseudomonas aeruginosa.Journal of bacteriology · 2017Article
- Two-component systems required for virulence in Pseudomonas aeruginosa.FEMS microbiology letters · 2017Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial chemosensory signal transduction systems that regulate motility by type IV pili (T4P) can be markedly more complex than related flagellum-based chemotaxis systems. In T4P-based systems, the CheA kinase often contains numerous potential sites of phosphorylation, but the signaling mechanisms of these systems are unknown. In Pseudomonas aeruginosa, the Pil-Chp system regulates T4P-mediated twitching motility and cAMP levels, both of which play roles in pathogenesis. The Pil-Chp histidine kinase (ChpA) has eight "Xpt" domains; six are canonical histidine-containing phosphotransfer (Hpt) domains and two have a threonine (Tpt) or serine (Spt) in place of the histidine. Additionally, there are two stand-alone receiver domains (PilG and PilH) and a ChpA C-terminal receiver domain (ChpArec). Here, we demonstrate that the ChpA Xpts are functionally divided into three categories as follows: (i) those phosphorylated with ATP (Hpt4-6); (ii) those reversibly phosphorylated by ChpArec (Hpt2-6), and (iii) those with no detectable phosphorylation (Hpt1, Spt, and Tpt). There was rapid phosphotransfer from Hpt2-6 to ChpArec and from Hpt3 to PilH, whereas transfer to PilG was slower. ChpArec also had a rapid rate of autodephosphorylation. The biochemical results together with in vivo cAMP and twitching phenotypes of key ChpA phosphorylation site point mutants supported a scheme whereby ChpArec functions both as a phosphate sink and a phosphotransfer element linking Hpt4-6 to Hpt2-3. Hpt2 and Hpt3 are likely the dominant sources of phosphoryl groups for PilG and PilH, respectively. The data are synthesized in a signaling circuit that contains fundamental features of two-component phosphorelays.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.