ArticleNucleic acids research2024
Molecular mechanism of the one-component regulator RccR on bacterial metabolism and virulence.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Mechanism of NanR transcriptional activation of sialic acid metabolism in Streptococcus pneumoniae.Nucleic acids research · 2026Article
- Characterization of two exoUBMC microbiology · 2026Article
- Within-host adaptation mutations associated with persistent colonization ofFrontiers in cellular and infection microbiology · 2026Article
- The CsWRKY50-CsREM1-CsTSⅠ module inhibits theanine biosynthesis in tea plants under drought stress.Plant physiology · 2025Article
- The Functional Characterization of the 6-Phosphogluconate Dehydratase Operon in 2-Ketogluconic Acid Industrial Producing StrainFoods (Basel, Switzerland) · 2024Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
The regulation of carbon metabolism and virulence is critical for the rapid adaptation of pathogenic bacteria to host conditions. In Pseudomonas aeruginosa, RccR is a transcriptional regulator of genes involved in primary carbon metabolism and is associated with bacterial resistance and virulence, although the exact mechanism is unclear. Our study demonstrates that PaRccR is a direct repressor of the transcriptional regulator genes mvaU and algU. Biochemical and structural analyses reveal that PaRccR can switch its DNA recognition mode through conformational changes triggered by KDPG binding or release. Mutagenesis and functional analysis underscore the significance of allosteric communication between the SIS domain and the DBD domain. Our findings suggest that, despite its overall structural similarity to other bacterial RpiR-type regulators, RccR displays a more complex regulatory element binding mode induced by ligands and a unique regulatory mechanism.
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Registered trials
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