ArticleNucleic acids research2009
The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Functional role of 18 LysR-Type transcriptional regulators of Salmonella enterica serovar Typhi.PloS one · 2025Article
- A bacterial transcription activator dedicated to the expression of the enzyme catalyzing the first committed step in fatty acid biosynthesis.Nucleic acids research · 2024Article
- Fundamentals and Exceptions of the LysR-type Transcriptional Regulators.ACS synthetic biology · 2024Review
- SstF, a novel sulforaphane-sensing transcription factor of Xanthomonas campestris, is required for sulforaphane tolerance and virulence.Molecular plant pathology · 2023Article
- Article
- Pneumococcal capsule expression is controlled through a conserved, distal cis-regulatory element during infection.PLoS pathogens · 2023Article
- Enhancing DNT Detection by a Bacterial Bioreporter: Directed Evolution of the Transcriptional Activator YhaJ.Frontiers in bioengineering and biotechnology · 2022Article
- Structural dynamics in the evolution of a bilobed protein scaffold.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A novel LysR-type regulator negatively affects biosynthesis of the immunosuppressant brasilicardin.Engineering in life sciences · 2021Article
- Assembly and regulation of the chlorhexidine-specific efflux pump AceI.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Regulation of γ-Aminobutyrate (GABA) Utilization inFrontiers in microbiology · 2020Article
- DbdR, a New Member of the LysR Family of Transcriptional Regulators, Coordinately Controls Four Promoters in the Thauera aromatica AR-1 3,5-Dihydroxybenzoate Anaerobic Degradation Pathway.Applied and environmental microbiology · 2019Article
- The evolution of Bordetella pertussis has selected for mutations of acr that lead to sensitivity to hydrophobic molecules and fatty acids.Emerging microbes & infections · 2019Article
- CrgA Protein Represses AlkB2 Monooxygenase and Regulates the Degradation of Medium-to-Long-ChainFrontiers in microbiology · 2019Article
- Crystal structure of the ligand-binding domain of a LysR-type transcriptional regulator: transcriptional activation via a rotary switch.Molecular microbiology · 2018Article
- Cell-Wall Recycling of the Gram-Negative Bacteria and the Nexus to Antibiotic Resistance.Chemical reviews · 2018Review
- VqsA, a Novel LysR-Type Transcriptional Regulator, Coordinates Quorum Sensing (QS) and Is Controlled by QS To Regulate Virulence in the Pathogen Vibrio alginolyticus.Applied and environmental microbiology · 2018Article
- Regulation of carbohydrate degradation pathways in Pseudomonas involves a versatile set of transcriptional regulators.Microbial biotechnology · 2018Review
- Coordinating carbon and nitrogen metabolic signaling through the cyanobacterial global repressor NdhR.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Regulator LdhR and d-Lactate Dehydrogenase LdhA of Burkholderia multivorans Play Roles in Carbon Overflow and in Planktonic Cellular Aggregate Formation.Applied and environmental microbiology · 2017Article
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8 authors.
Funding
Abstract
LysR-type transcriptional regulators (LTTRs) form the largest family of bacterial regulators acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes. The LTTR, CrgA, from the human pathogen Neisseria meningitidis, is upregulated during bacterial-host cell contact. Here, we report the crystal structures of both regulatory domain and full-length CrgA, the first of a novel subclass of LTTRs that form octameric rings. Non-denaturing mass spectrometry analysis and analytical ultracentrifugation established that the octameric form of CrgA is the predominant species in solution in both the presence and absence of an oligonucleotide encompassing the CrgA-binding sequence. Furthermore, analysis of the isolated CrgA-DNA complex by mass spectrometry showed stabilization of a double octamer species upon DNA binding. Based on the observed structure and the mass spectrometry findings, a model is proposed in which a hexadecameric array of two CrgA oligomers binds to its DNA target site.
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