Structure of the response regulator ChrA in the haem-sensing two-component system of<i>Corynebacterium diphtheriae</i>

Doi, Atsushi; Nakamura, H.; Shiro, Yoshitsugu; Sugimoto, Hiroshi

doi:10.1107/s2053230x15009838

Cited by 5 publications

(3 citation statements)

References 22 publications

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“…4A). The N-terminal REC domain and the C-terminal effector domain each exhibits the same fold as those reported for other DNA binding RRs (24). The linker region contained two  helices (6A and 6B) in the C222 1 data.…”

Section: Crystal and Solution Structures Of Full-length Fixjmentioning

confidence: 56%

Architecture of the complete oxygen-sensing FixL-FixJ two-component signal transduction system

et al. 2018

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The symbiotic nitrogen-fixing bacterium is critical to the agro-industrial production of soybean because it enables the production of high yields of soybeans with little use of nitrogenous fertilizers. The FixL and FixJ two-component system (TCS) of this bacterium ensures that nitrogen fixation is only stimulated under conditions of low oxygen. When it is not bound to oxygen, the histidine kinase FixL undergoes autophosphorylation and transfers phosphate from adenosine triphosphate (ATP) to the response regulator FixJ, which, in turn, stimulates the expression of genes required for nitrogen fixation. We purified full-length FixL and FixJ proteins and defined their structures individually and in complex using small-angle x-ray scattering, crystallographic, and in silico modeling techniques. Comparison of active and inactive forms of FixL suggests that intramolecular signal transduction is driven by local changes in the sensor domain and in the coiled-coil region connecting the sensor and histidine kinase domains. We also found that FixJ exhibits conformational plasticity not only in the monomeric state but also in tetrameric complexes with FixL during phosphotransfer. This structural characterization of a complete TCS contributes both a mechanistic and evolutionary understanding to TCS signal relay, specifically in the context of the control of nitrogen fixation in root nodules.

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Section: Crystal and Solution Structures Of Full-length Fixjmentioning

confidence: 56%

Architecture of the complete oxygen-sensing FixL-FixJ two-component signal transduction system

et al. 2018

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“…A search for homologous structures based on sequence conservation revealed existing PDB structures of known full‐length FixJ/NarL regulators that are similar to E. coli RcsB. The highest ranked proteins based on sequence identity are the response regulator ChrA in a haem‐sensing two‐component system from Corynebacterium diphtheria (PDB ID 4YN8), the vancomycin‐resistance‐associated response regulator VraR from Staphylococcus aureus (PDB ID 4GVP), and the nitrate/nitrite response regulator NarL from E. coli (PDB ID 1RNL). All these response regulators contain DNA‐binding and receiver domains connected by a long inter‐domain linker.…”

Section: Resultsmentioning

confidence: 99%

Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli

et al. 2016

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RcsB, the transcription-associated response regulator of the Rcs phosphorelay twocomponent signal transduction system, activates cell stress responses associated with desiccation, cell wall biosynthesis, cell division, virulence, biofilm formation, and antibiotic resistance in enteric bacterial pathogens. RcsB belongs to the FixJ/NarL family of transcriptional regulators, which are characterized by a highly conserved C-terminal DNA-binding domain. The N-terminal domain of RcsB belongs to the family of two-component receiver domains. This receiver domain contains the phosphoacceptor site and participates in RcsB dimer formation; it also contributes to dimer formation with other transcription factor partners. Here, we describe the crystal structure of the Escherichia coli RcsB receiver domain in its nonphosphorylated state. The structure reveals important molecular details of phosphorylation-independent dimerization of RcsB and has implication for the formation of heterodimers.

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“…1 A). ChrA consists of an N-terminal regulatory domain and a C-terminal DNA-binding region, and the linker region of the N-terminal could create a dimerization interface binding DNA when receiving a heme-sensing signal [ 61 ]. Deletion of chrAB failed to trigger the expression of hrtAB under heme pressure, and mutations in hrtAB cause high heme sensitivity and the accumulation of cytoplasmic heme [ 56 , 62 ].…”

Section: Strategies Of Gram-positive Bacteria To Resist Heme Toxicitymentioning

confidence: 99%

Heme acquisition and tolerance in Gram-positive model bacteria: An orchestrated balance

Wang

et al. 2023

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Structure of the response regulator ChrA in the haem-sensing two-component system ofCorynebacterium diphtheriae

Cited by 5 publications

References 22 publications

Architecture of the complete oxygen-sensing FixL-FixJ two-component signal transduction system

Architecture of the complete oxygen-sensing FixL-FixJ two-component signal transduction system

Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli

Heme acquisition and tolerance in Gram-positive model bacteria: An orchestrated balance

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