ArticlePloS one2013
The Pseudomonas aeruginosa catabolite repression control protein Crc is devoid of RNA binding activity.
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 26 papers.
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Who cites it
26 citing papers in PubMed, 55 citations in OpenAlex.
- The Catabolite Repression Control Protein Crc Regulates the Type III Secretion System Through the Adenylate Cyclase CyaB inMicroorganisms · 2025Article
- The link of carbon catabolite repression elements, small RNAs CrcY and CrcZ and polyhydroxyalkanoate metabolism in Pseudomonas putida KT2440.Biotechnology for biofuels and bioproducts · 2025Article
- Broadly conserved FlgV controls flagellar assembly and Borrelia burgdorferi dissemination in mice.Nature communications · 2024Article
- Broadly conserved FlgV controls flagellar assembly andbioRxiv : the preprint server for biology · 2024Article
- Translational regulation by Hfq-Crc assemblies emerges from polymorphic ribonucleoprotein folding.The EMBO journal · 2023Article
- Catabolite repression control protein antagonist, a novel player inFrontiers in microbiology · 2023Article
- Regulation of hierarchical carbon substrate utilization, nitrogen fixation, and root colonization by the Hfq/Crc/CrcZY genes iniScience · 2022Article
- Role of Two-Component System Networks in Pseudomonas aeruginosa Pathogenesis.Advances in experimental medicine and biology · 2022Article
- Rewiring of Gene Expression inFrontiers in microbiology · 2022Article
- Stabilization of Hfq-mediated translational repression by the co-repressor Crc in Pseudomonas aeruginosa.Nucleic acids research · 2021Article
- Impacts of Small RNAs and Their Chaperones on Bacterial Pathogenicity.Frontiers in cellular and infection microbiology · 2021Review
- Hfq-Assisted RsmA Regulation Is Central toFrontiers in microbiology · 2020Article
- Full Transcriptomic Response ofFrontiers in microbiology · 2020Article
- Rewiring the functional complexity between Crc, Hfq and sRNAs to regulate carbon catabolite repression in Pseudomonas.World journal of microbiology & biotechnology · 2019Review
- Fitting Pieces into the Puzzle ofJournal of bacteriology · 2019Review
- Article
- The absence of SigX results in impaired carbon metabolism and membrane fluidity in Pseudomonas aeruginosa.Scientific reports · 2018Article
- Pervasive Targeting of Nascent Transcripts by Hfq.Cell reports · 2018Article
- Interplay between the catabolite repression control protein Crc, Hfq and RNA in Hfq-dependent translational regulation in Pseudomonas aeruginosa.Nucleic acids research · 2018Article
- Transcription factor levels enable metabolic diversification of single cells of environmental bacteria.The ISME journal · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Crc protein has been shown to mediate catabolite repression control in Pseudomonas, leading to a preferential assimilation of carbon sources. It has been suggested that Crc acts as a translational repressor of mRNAs, encoding functions involved in uptake and breakdown of different carbon sources. Moreover, the regulatory RNA CrcZ, the level of which is increased in the presence of less preferred carbon sources, was suggested to bind to and sequester Crc, resulting in a relief of catabolite repression. Here, we determined the crystal structure of Pseudomonas aeruginosa Crc, a member of apurinic/apyrimidinic (AP) endonuclease family, at 1.8 Å. Although Crc displays high sequence similarity with its orthologs, there are amino acid alterations in the area corresponding to the active site in AP proteins. Unlike typical AP endonuclease family proteins, Crc has a reduced overall positive charge and the conserved positively charged amino-acid residues of the DNA-binding surface of AP proteins are partially substituted by negatively charged, polar and hydrophobic residues. Crc protein purified to homogeneity from P. aeruginosa did neither display DNase activity, nor did it bind to previously identified RNA substrates. Rather, the RNA chaperone Hfq was identified as a contaminant in His-tagged Crc preparations purified by one step Ni-affinity chromatography from Escherichia coli, and was shown to account for the RNA binding activity observed with the His-Crc preparations. Taken together, these data challenge a role of Crc as a direct translational repressor in carbon catabolite repression in P. aeruginosa.
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