ArticleFrontiers in microbiology2016
Functional Analysis of the Citrate Activator CitO from Enterococcus faecalis Implicates a Divalent Metal in Ligand Binding.
Article in Frontiers in microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- One size does not fit all - Trehalose metabolism byMicrobial genomics · 2023Article
- GntR-like SCO3932 Protein Provides a Link between Actinomycete Integrative and Conjugative Elements and Secondary Metabolism.International journal of molecular sciences · 2021Article
- Identification of Potential Citrate Metabolism Pathways inMicroorganisms · 2021Article
- Transcription factor allosteric regulation through substrate coordination to zinc.NAR genomics and bioinformatics · 2021Article
- Structural and Functional Analyses of the Transcription Repressor DgoR FromFrontiers in microbiology · 2020Article
- A GntR-Like Transcription Factor HypR Regulates Expression of Genes Associated With L-Hydroxyproline Utilization inFrontiers in microbiology · 2019Article
- Implications of the expression of Enterococcus faecalis citrate fermentation genes during infection.PloS one · 2018Article
- Genetic Engineering ofFrontiers in microbiology · 2018Article
- Metallochaperones and metalloregulation in bacteria.Essays in biochemistry · 2017Review
- Identification of the Tolfenamic Acid Binding Pocket in PrbP fromFrontiers in microbiology · 2017Article
- Expanding the Cyanobacterial Nitrogen Regulatory Network: The GntR-Like Regulator PlmA Interacts with the PII-PipX Complex.Frontiers in microbiology · 2016Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The regulator of citrate metabolism, CitO, from Enterococcus faecalis belongs to the FCD family within the GntR superfamily. In the presence of citrate, CitO binds to cis-acting sequences located upstream of the cit promoters inducing the expression of genes involved in citrate utilization. The quantification of the molecular binding affinities, performed by isothermal titration calorimetry (ITC), indicated that CitO has a high affinity for citrate (K D = 1.2 ± 0.2 μM), while it did not recognize other metabolic intermediates. Based on a structural model of CitO where a putative small molecule and a metal binding site were identified, it was hypothesized that the metal ion is required for citrate binding. In agreement with this model, citrate binding to CitO sharply decreased when the protein was incubated with EDTA. This effect was reverted by the addition of Ni(2+), and Zn(2+) to a lesser extent. Structure-based site-directed mutagenesis was conducted and it was found that changes to alanine in residues Arg97 and His191 resulted in decreased binding affinities for citrate, as determined by EMSA and ITC. Further assays using lacZ fusions confirmed that these residues in CitO are involved in sensing citrate in vivo. These results indicate that the molecular modifications induced by a ligand and a metal binding in the C-terminal domain of CitO are required for optimal DNA binding activity, and consequently, transcriptional activation.
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