Review



chromobacterium subtsugae  (ATCC)


Bioz Verified Symbol ATCC is a verified supplier
Bioz Manufacturer Symbol ATCC manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 96

    Structured Review

    ATCC chromobacterium subtsugae
    (A) Structural model of P. aeruginosa RhlR, highlighting the modular architecture that defines LuxR-type receptors: an N-terminal acyl-homoserine lactone (AHL) ligand-binding domain (LBD; turquoise) and a C-terminal helix-turn-helix (HTH) DNA-binding domain (DBD; yellow). The solvent-accessible volume of the LBD ligand-binding pocket is shown in light pink to provide structural context. Structures are derived from PDB IDs 8DQ0 and 8DQ1 , and all structure images were generated using ChimeraX. (B) Panel of AHL signal molecules recognized by the cognate receptors as in panel C. C4-HSL; P. aeruginosa ; RhlR, C6-HSL; C. <t>subtsugae</t> ; CviR, 3OC8-HSL; A. tumefaciens ; TraR, 3OC12-HSL; LasR; 3OHC12-HSL; A. baumannii ; AbaR. (C) Multiple sequence alignment (MSA) of LuxR-type receptors discussed in this review, spanning residues 44–72, which correspond to a conserved portion of the LBD. Amino acids are colored by physicochemical properties (positive, negative, polar, and non-polar, as indicated). A maximum-likelihood phylogenetic tree based on full-length sequences is shown to the left of the alignment. (D) Sequence alignment of the HTH DNA binding domains (residues 198–217) from the same set of receptors shown in panel B. The phylogenetic tree is omitted for clarity. Conserved residues within the HTH motif are denoted with an asterisk.
    Chromobacterium Subtsugae, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 311 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/chromobacterium+subtsugae+martin+et+al/Chromobacterium+subtsugae+Martin+et+al/pmc13043044-119-1-6
    Average 96 stars, based on 311 article reviews
    chromobacterium subtsugae - by Bioz Stars, 2026-10
    96/100 stars

    Images

    1) Product Images from "Expanding the LuxR-type receptor functional repertoire: Protein-protein interactions in quorum sensing regulation"

    Article Title: Expanding the LuxR-type receptor functional repertoire: Protein-protein interactions in quorum sensing regulation

    Journal: PLOS Pathogens

    doi: 10.1371/journal.ppat.1014091

    (A) Structural model of P. aeruginosa RhlR, highlighting the modular architecture that defines LuxR-type receptors: an N-terminal acyl-homoserine lactone (AHL) ligand-binding domain (LBD; turquoise) and a C-terminal helix-turn-helix (HTH) DNA-binding domain (DBD; yellow). The solvent-accessible volume of the LBD ligand-binding pocket is shown in light pink to provide structural context. Structures are derived from PDB IDs 8DQ0 and 8DQ1 , and all structure images were generated using ChimeraX. (B) Panel of AHL signal molecules recognized by the cognate receptors as in panel C. C4-HSL; P. aeruginosa ; RhlR, C6-HSL; C. subtsugae ; CviR, 3OC8-HSL; A. tumefaciens ; TraR, 3OC12-HSL; LasR; 3OHC12-HSL; A. baumannii ; AbaR. (C) Multiple sequence alignment (MSA) of LuxR-type receptors discussed in this review, spanning residues 44–72, which correspond to a conserved portion of the LBD. Amino acids are colored by physicochemical properties (positive, negative, polar, and non-polar, as indicated). A maximum-likelihood phylogenetic tree based on full-length sequences is shown to the left of the alignment. (D) Sequence alignment of the HTH DNA binding domains (residues 198–217) from the same set of receptors shown in panel B. The phylogenetic tree is omitted for clarity. Conserved residues within the HTH motif are denoted with an asterisk.
    Figure Legend Snippet: (A) Structural model of P. aeruginosa RhlR, highlighting the modular architecture that defines LuxR-type receptors: an N-terminal acyl-homoserine lactone (AHL) ligand-binding domain (LBD; turquoise) and a C-terminal helix-turn-helix (HTH) DNA-binding domain (DBD; yellow). The solvent-accessible volume of the LBD ligand-binding pocket is shown in light pink to provide structural context. Structures are derived from PDB IDs 8DQ0 and 8DQ1 , and all structure images were generated using ChimeraX. (B) Panel of AHL signal molecules recognized by the cognate receptors as in panel C. C4-HSL; P. aeruginosa ; RhlR, C6-HSL; C. subtsugae ; CviR, 3OC8-HSL; A. tumefaciens ; TraR, 3OC12-HSL; LasR; 3OHC12-HSL; A. baumannii ; AbaR. (C) Multiple sequence alignment (MSA) of LuxR-type receptors discussed in this review, spanning residues 44–72, which correspond to a conserved portion of the LBD. Amino acids are colored by physicochemical properties (positive, negative, polar, and non-polar, as indicated). A maximum-likelihood phylogenetic tree based on full-length sequences is shown to the left of the alignment. (D) Sequence alignment of the HTH DNA binding domains (residues 198–217) from the same set of receptors shown in panel B. The phylogenetic tree is omitted for clarity. Conserved residues within the HTH motif are denoted with an asterisk.

    Techniques Used: Ligand Binding Assay, Binding Assay, Solvent, Derivative Assay, Generated, Sequencing

    LuxR-type QS receptors (light-green ovals) are subject to regulation by a range of protein interaction partners (purple ovals), which modulate receptor function through distinct mechanisms. Negative regulators inhibit LuxR-type receptor function by disrupting dimerization, decreasing receptor stability, and inhibiting DNA binding. Representative examples include TraM-TraR ( A. tumefaciens ) , QscR-LasR/RhlR QteE-LasR/RhlR, Aqs1-LasR (all P.s aeruginosa ), and VioS-CviR ( C. subtsugae ). Dual or context-dependent regulators modify LuxR-type receptor activity in a promoter-, ligand-, or environmental-dependent manner. Examples include PqsE-RhlR ( P. aeruginosa ) and BlsA-AbaR ( A. baumannii ), which increase DNA binding affinity and/or transcriptional output under specific conditions. Global regulators modulate LuxR-type receptor function through transcriptional engagement or post-translational control, including RNA polymerase-mediated activation and protease-dependent receptor degradation. Created in BioRender. Paczkowski, J. (2026) https://BioRender.com/akj8r1w .
    Figure Legend Snippet: LuxR-type QS receptors (light-green ovals) are subject to regulation by a range of protein interaction partners (purple ovals), which modulate receptor function through distinct mechanisms. Negative regulators inhibit LuxR-type receptor function by disrupting dimerization, decreasing receptor stability, and inhibiting DNA binding. Representative examples include TraM-TraR ( A. tumefaciens ) , QscR-LasR/RhlR QteE-LasR/RhlR, Aqs1-LasR (all P.s aeruginosa ), and VioS-CviR ( C. subtsugae ). Dual or context-dependent regulators modify LuxR-type receptor activity in a promoter-, ligand-, or environmental-dependent manner. Examples include PqsE-RhlR ( P. aeruginosa ) and BlsA-AbaR ( A. baumannii ), which increase DNA binding affinity and/or transcriptional output under specific conditions. Global regulators modulate LuxR-type receptor function through transcriptional engagement or post-translational control, including RNA polymerase-mediated activation and protease-dependent receptor degradation. Created in BioRender. Paczkowski, J. (2026) https://BioRender.com/akj8r1w .

    Techniques Used: Binding Assay, Activity Assay, Control, Activation Assay

    Related Articles

    Comparison:

    Article Title: Digital Printing of Nanoenabled Enzymes on Textiles: An Integrated Antimicrobial and Antibiofilm Approach
    Article Snippet: oparticles Finishing Technologies to Obtain Antibacterial Properties of Cotton Fabric. Fibers Polym. 2022, 23 (9), 2606. (42) Harrison, A. M.; Soby, S. D. Reclassification of Chromobacterium Violaceum ATCC 31532 and Its Quorum Biosensor Mutant CV026 to Chromobacterium Subtsugae. AMB Express 2020, 10 (1), 202. (43) Rampersad, S. N. Multiple Applications of Alamar Blue as an Indicator of Metabolic Fu

    Mutagenesis:

    Article Title: Digital Printing of Nanoenabled Enzymes on Textiles: An Integrated Antimicrobial and Antibiofilm Approach
    Article Snippet: oparticles Finishing Technologies to Obtain Antibacterial Properties of Cotton Fabric. Fibers Polym. 2022, 23 (9), 2606. (42) Harrison, A. M.; Soby, S. D. Reclassification of Chromobacterium Violaceum ATCC 31532 and Its Quorum Biosensor Mutant CV026 to Chromobacterium Subtsugae. AMB Express 2020, 10 (1), 202. (43) Rampersad, S. N. Multiple Applications of Alamar Blue as an Indicator of Metabolic Fu

    Inhibition:

    Article Title: Digital Printing of Nanoenabled Enzymes on Textiles: An Integrated Antimicrobial and Antibiofilm Approach
    Article Snippet: oparticles Finishing Technologies to Obtain Antibacterial Properties of Cotton Fabric. Fibers Polym. 2022, 23 (9), 2606. (42) Harrison, A. M.; Soby, S. D. Reclassification of Chromobacterium Violaceum ATCC 31532 and Its Quorum Biosensor Mutant CV026 to Chromobacterium Subtsugae. AMB Express 2020, 10 (1), 202. (43) Rampersad, S. N. Multiple Applications of Alamar Blue as an Indicator of Metabolic Fu

    Activity Assay:

    Article Title: Digital Printing of Nanoenabled Enzymes on Textiles: An Integrated Antimicrobial and Antibiofilm Approach
    Article Snippet: oparticles Finishing Technologies to Obtain Antibacterial Properties of Cotton Fabric. Fibers Polym. 2022, 23 (9), 2606. (42) Harrison, A. M.; Soby, S. D. Reclassification of Chromobacterium Violaceum ATCC 31532 and Its Quorum Biosensor Mutant CV026 to Chromobacterium Subtsugae. AMB Express 2020, 10 (1), 202. (43) Rampersad, S. N. Multiple Applications of Alamar Blue as an Indicator of Metabolic Fu

    Concentration Assay:

    Article Title: Digital Printing of Nanoenabled Enzymes on Textiles: An Integrated Antimicrobial and Antibiofilm Approach
    Article Snippet: oparticles Finishing Technologies to Obtain Antibacterial Properties of Cotton Fabric. Fibers Polym. 2022, 23 (9), 2606. (42) Harrison, A. M.; Soby, S. D. Reclassification of Chromobacterium Violaceum ATCC 31532 and Its Quorum Biosensor Mutant CV026 to Chromobacterium Subtsugae. AMB Express 2020, 10 (1), 202. (43) Rampersad, S. N. Multiple Applications of Alamar Blue as an Indicator of Metabolic Fu

    Cell Culture:

    Article Title: Digital Printing of Nanoenabled Enzymes on Textiles: An Integrated Antimicrobial and Antibiofilm Approach
    Article Snippet: oparticles Finishing Technologies to Obtain Antibacterial Properties of Cotton Fabric. Fibers Polym. 2022, 23 (9), 2606. (42) Harrison, A. M.; Soby, S. D. Reclassification of Chromobacterium Violaceum ATCC 31532 and Its Quorum Biosensor Mutant CV026 to Chromobacterium Subtsugae. AMB Express 2020, 10 (1), 202. (43) Rampersad, S. N. Multiple Applications of Alamar Blue as an Indicator of Metabolic Fu

    Incubation:

    Article Title: Digital Printing of Nanoenabled Enzymes on Textiles: An Integrated Antimicrobial and Antibiofilm Approach
    Article Snippet: oparticles Finishing Technologies to Obtain Antibacterial Properties of Cotton Fabric. Fibers Polym. 2022, 23 (9), 2606. (42) Harrison, A. M.; Soby, S. D. Reclassification of Chromobacterium Violaceum ATCC 31532 and Its Quorum Biosensor Mutant CV026 to Chromobacterium Subtsugae. AMB Express 2020, 10 (1), 202. (43) Rampersad, S. N. Multiple Applications of Alamar Blue as an Indicator of Metabolic Fu

    Binding Assay:

    Article Title: Digital Printing of Nanoenabled Enzymes on Textiles: An Integrated Antimicrobial and Antibiofilm Approach
    Article Snippet: oparticles Finishing Technologies to Obtain Antibacterial Properties of Cotton Fabric. Fibers Polym. 2022, 23 (9), 2606. (42) Harrison, A. M.; Soby, S. D. Reclassification of Chromobacterium Violaceum ATCC 31532 and Its Quorum Biosensor Mutant CV026 to Chromobacterium Subtsugae. AMB Express 2020, 10 (1), 202. (43) Rampersad, S. N. Multiple Applications of Alamar Blue as an Indicator of Metabolic Fu

    High Performance Liquid Chromatography:

    Article Title: Digital Printing of Nanoenabled Enzymes on Textiles: An Integrated Antimicrobial and Antibiofilm Approach
    Article Snippet: oparticles Finishing Technologies to Obtain Antibacterial Properties of Cotton Fabric. Fibers Polym. 2022, 23 (9), 2606. (42) Harrison, A. M.; Soby, S. D. Reclassification of Chromobacterium Violaceum ATCC 31532 and Its Quorum Biosensor Mutant CV026 to Chromobacterium Subtsugae. AMB Express 2020, 10 (1), 202. (43) Rampersad, S. N. Multiple Applications of Alamar Blue as an Indicator of Metabolic Fu

    Stable Transfection:

    Article Title: Digital Printing of Nanoenabled Enzymes on Textiles: An Integrated Antimicrobial and Antibiofilm Approach
    Article Snippet: oparticles Finishing Technologies to Obtain Antibacterial Properties of Cotton Fabric. Fibers Polym. 2022, 23 (9), 2606. (42) Harrison, A. M.; Soby, S. D. Reclassification of Chromobacterium Violaceum ATCC 31532 and Its Quorum Biosensor Mutant CV026 to Chromobacterium Subtsugae. AMB Express 2020, 10 (1), 202. (43) Rampersad, S. N. Multiple Applications of Alamar Blue as an Indicator of Metabolic Fu

    Derivative Assay:

    Article Title: Digital Printing of Nanoenabled Enzymes on Textiles: An Integrated Antimicrobial and Antibiofilm Approach
    Article Snippet: oparticles Finishing Technologies to Obtain Antibacterial Properties of Cotton Fabric. Fibers Polym. 2022, 23 (9), 2606. (42) Harrison, A. M.; Soby, S. D. Reclassification of Chromobacterium Violaceum ATCC 31532 and Its Quorum Biosensor Mutant CV026 to Chromobacterium Subtsugae. AMB Express 2020, 10 (1), 202. (43) Rampersad, S. N. Multiple Applications of Alamar Blue as an Indicator of Metabolic Fu

    SPR Assay:

    Article Title: Digital Printing of Nanoenabled Enzymes on Textiles: An Integrated Antimicrobial and Antibiofilm Approach
    Article Snippet: oparticles Finishing Technologies to Obtain Antibacterial Properties of Cotton Fabric. Fibers Polym. 2022, 23 (9), 2606. (42) Harrison, A. M.; Soby, S. D. Reclassification of Chromobacterium Violaceum ATCC 31532 and Its Quorum Biosensor Mutant CV026 to Chromobacterium Subtsugae. AMB Express 2020, 10 (1), 202. (43) Rampersad, S. N. Multiple Applications of Alamar Blue as an Indicator of Metabolic Fu



    Similar Products

    96
    ATCC chromobacterium subtsugae
    (A) Structural model of P. aeruginosa RhlR, highlighting the modular architecture that defines LuxR-type receptors: an N-terminal acyl-homoserine lactone (AHL) ligand-binding domain (LBD; turquoise) and a C-terminal helix-turn-helix (HTH) DNA-binding domain (DBD; yellow). The solvent-accessible volume of the LBD ligand-binding pocket is shown in light pink to provide structural context. Structures are derived from PDB IDs 8DQ0 and 8DQ1 , and all structure images were generated using ChimeraX. (B) Panel of AHL signal molecules recognized by the cognate receptors as in panel C. C4-HSL; P. aeruginosa ; RhlR, C6-HSL; C. <t>subtsugae</t> ; CviR, 3OC8-HSL; A. tumefaciens ; TraR, 3OC12-HSL; LasR; 3OHC12-HSL; A. baumannii ; AbaR. (C) Multiple sequence alignment (MSA) of LuxR-type receptors discussed in this review, spanning residues 44–72, which correspond to a conserved portion of the LBD. Amino acids are colored by physicochemical properties (positive, negative, polar, and non-polar, as indicated). A maximum-likelihood phylogenetic tree based on full-length sequences is shown to the left of the alignment. (D) Sequence alignment of the HTH DNA binding domains (residues 198–217) from the same set of receptors shown in panel B. The phylogenetic tree is omitted for clarity. Conserved residues within the HTH motif are denoted with an asterisk.
    Chromobacterium Subtsugae, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/chromobacterium+subtsugae+martin+et+al/Chromobacterium+subtsugae+Martin+et+al/pmc13043044-119-1-6
    Average 96 stars, based on 1 article reviews
    chromobacterium subtsugae - by Bioz Stars, 2026-10
    96/100 stars
      Buy from Supplier

    96
    ATCC chromobacterium subtsugae martin et al
    (A) Structural model of P. aeruginosa RhlR, highlighting the modular architecture that defines LuxR-type receptors: an N-terminal acyl-homoserine lactone (AHL) ligand-binding domain (LBD; turquoise) and a C-terminal helix-turn-helix (HTH) DNA-binding domain (DBD; yellow). The solvent-accessible volume of the LBD ligand-binding pocket is shown in light pink to provide structural context. Structures are derived from PDB IDs 8DQ0 and 8DQ1 , and all structure images were generated using ChimeraX. (B) Panel of AHL signal molecules recognized by the cognate receptors as in panel C. C4-HSL; P. aeruginosa ; RhlR, C6-HSL; C. <t>subtsugae</t> ; CviR, 3OC8-HSL; A. tumefaciens ; TraR, 3OC12-HSL; LasR; 3OHC12-HSL; A. baumannii ; AbaR. (C) Multiple sequence alignment (MSA) of LuxR-type receptors discussed in this review, spanning residues 44–72, which correspond to a conserved portion of the LBD. Amino acids are colored by physicochemical properties (positive, negative, polar, and non-polar, as indicated). A maximum-likelihood phylogenetic tree based on full-length sequences is shown to the left of the alignment. (D) Sequence alignment of the HTH DNA binding domains (residues 198–217) from the same set of receptors shown in panel B. The phylogenetic tree is omitted for clarity. Conserved residues within the HTH motif are denoted with an asterisk.
    Chromobacterium Subtsugae Martin Et Al, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/chromobacterium+subtsugae+martin+et+al/Chromobacterium+subtsugae+Martin+et+al/custom%4031532%4041698559
    Average 96 stars, based on 1 article reviews
    chromobacterium subtsugae martin et al - by Bioz Stars, 2026-10
    96/100 stars
      Buy from Supplier

    96
    ATCC c violaceum atcc 31532
    (A) Structural model of P. aeruginosa RhlR, highlighting the modular architecture that defines LuxR-type receptors: an N-terminal acyl-homoserine lactone (AHL) ligand-binding domain (LBD; turquoise) and a C-terminal helix-turn-helix (HTH) DNA-binding domain (DBD; yellow). The solvent-accessible volume of the LBD ligand-binding pocket is shown in light pink to provide structural context. Structures are derived from PDB IDs 8DQ0 and 8DQ1 , and all structure images were generated using ChimeraX. (B) Panel of AHL signal molecules recognized by the cognate receptors as in panel C. C4-HSL; P. aeruginosa ; RhlR, C6-HSL; C. <t>subtsugae</t> ; CviR, 3OC8-HSL; A. tumefaciens ; TraR, 3OC12-HSL; LasR; 3OHC12-HSL; A. baumannii ; AbaR. (C) Multiple sequence alignment (MSA) of LuxR-type receptors discussed in this review, spanning residues 44–72, which correspond to a conserved portion of the LBD. Amino acids are colored by physicochemical properties (positive, negative, polar, and non-polar, as indicated). A maximum-likelihood phylogenetic tree based on full-length sequences is shown to the left of the alignment. (D) Sequence alignment of the HTH DNA binding domains (residues 198–217) from the same set of receptors shown in panel B. The phylogenetic tree is omitted for clarity. Conserved residues within the HTH motif are denoted with an asterisk.
    C Violaceum Atcc 31532, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/chromobacterium+subtsugae+martin+et+al/Chromobacterium+subtsugae+Martin+et+al/pm41572086-133-0-2
    Average 96 stars, based on 1 article reviews
    c violaceum atcc 31532 - by Bioz Stars, 2026-10
    96/100 stars
      Buy from Supplier

    96
    ATCC c violaceum atcc
    (A) Structural model of P. aeruginosa RhlR, highlighting the modular architecture that defines LuxR-type receptors: an N-terminal acyl-homoserine lactone (AHL) ligand-binding domain (LBD; turquoise) and a C-terminal helix-turn-helix (HTH) DNA-binding domain (DBD; yellow). The solvent-accessible volume of the LBD ligand-binding pocket is shown in light pink to provide structural context. Structures are derived from PDB IDs 8DQ0 and 8DQ1 , and all structure images were generated using ChimeraX. (B) Panel of AHL signal molecules recognized by the cognate receptors as in panel C. C4-HSL; P. aeruginosa ; RhlR, C6-HSL; C. <t>subtsugae</t> ; CviR, 3OC8-HSL; A. tumefaciens ; TraR, 3OC12-HSL; LasR; 3OHC12-HSL; A. baumannii ; AbaR. (C) Multiple sequence alignment (MSA) of LuxR-type receptors discussed in this review, spanning residues 44–72, which correspond to a conserved portion of the LBD. Amino acids are colored by physicochemical properties (positive, negative, polar, and non-polar, as indicated). A maximum-likelihood phylogenetic tree based on full-length sequences is shown to the left of the alignment. (D) Sequence alignment of the HTH DNA binding domains (residues 198–217) from the same set of receptors shown in panel B. The phylogenetic tree is omitted for clarity. Conserved residues within the HTH motif are denoted with an asterisk.
    C Violaceum Atcc, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/chromobacterium+subtsugae+martin+et+al/Chromobacterium+subtsugae+Martin+et+al/pm41572086-132-0-2
    Average 96 stars, based on 1 article reviews
    c violaceum atcc - by Bioz Stars, 2026-10
    96/100 stars
      Buy from Supplier

    strain  (ATCC)
    96
    ATCC strain
    (A) Structural model of P. aeruginosa RhlR, highlighting the modular architecture that defines LuxR-type receptors: an N-terminal acyl-homoserine lactone (AHL) ligand-binding domain (LBD; turquoise) and a C-terminal helix-turn-helix (HTH) DNA-binding domain (DBD; yellow). The solvent-accessible volume of the LBD ligand-binding pocket is shown in light pink to provide structural context. Structures are derived from PDB IDs 8DQ0 and 8DQ1 , and all structure images were generated using ChimeraX. (B) Panel of AHL signal molecules recognized by the cognate receptors as in panel C. C4-HSL; P. aeruginosa ; RhlR, C6-HSL; C. <t>subtsugae</t> ; CviR, 3OC8-HSL; A. tumefaciens ; TraR, 3OC12-HSL; LasR; 3OHC12-HSL; A. baumannii ; AbaR. (C) Multiple sequence alignment (MSA) of LuxR-type receptors discussed in this review, spanning residues 44–72, which correspond to a conserved portion of the LBD. Amino acids are colored by physicochemical properties (positive, negative, polar, and non-polar, as indicated). A maximum-likelihood phylogenetic tree based on full-length sequences is shown to the left of the alignment. (D) Sequence alignment of the HTH DNA binding domains (residues 198–217) from the same set of receptors shown in panel B. The phylogenetic tree is omitted for clarity. Conserved residues within the HTH motif are denoted with an asterisk.
    Strain, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/chromobacterium+subtsugae+martin+et+al/Chromobacterium+subtsugae+Martin+et+al/pm41572086-246-13-16
    Average 96 stars, based on 1 article reviews
    strain - by Bioz Stars, 2026-10
    96/100 stars
      Buy from Supplier

    96
    ATCC atcc 31532
    (A) Structural model of P. aeruginosa RhlR, highlighting the modular architecture that defines LuxR-type receptors: an N-terminal acyl-homoserine lactone (AHL) ligand-binding domain (LBD; turquoise) and a C-terminal helix-turn-helix (HTH) DNA-binding domain (DBD; yellow). The solvent-accessible volume of the LBD ligand-binding pocket is shown in light pink to provide structural context. Structures are derived from PDB IDs 8DQ0 and 8DQ1 , and all structure images were generated using ChimeraX. (B) Panel of AHL signal molecules recognized by the cognate receptors as in panel C. C4-HSL; P. aeruginosa ; RhlR, C6-HSL; C. <t>subtsugae</t> ; CviR, 3OC8-HSL; A. tumefaciens ; TraR, 3OC12-HSL; LasR; 3OHC12-HSL; A. baumannii ; AbaR. (C) Multiple sequence alignment (MSA) of LuxR-type receptors discussed in this review, spanning residues 44–72, which correspond to a conserved portion of the LBD. Amino acids are colored by physicochemical properties (positive, negative, polar, and non-polar, as indicated). A maximum-likelihood phylogenetic tree based on full-length sequences is shown to the left of the alignment. (D) Sequence alignment of the HTH DNA binding domains (residues 198–217) from the same set of receptors shown in panel B. The phylogenetic tree is omitted for clarity. Conserved residues within the HTH motif are denoted with an asterisk.
    Atcc 31532, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/chromobacterium+subtsugae+martin+et+al/Chromobacterium+subtsugae+Martin+et+al/pm41572086-32-7-7
    Average 96 stars, based on 1 article reviews
    atcc 31532 - by Bioz Stars, 2026-10
    96/100 stars
      Buy from Supplier

    96
    ATCC c violaceum
    Quantitative determination of violacein inhibition in C. <t>violaceum</t> 12472 by sub-MICs of CMRE. Data is presented as mean of triplicates and bar denotes SD. Different letters above the bars indicate statistically significant differences among treatments ( p < 0.05). * depicts p ≤ 0.05 wrt to control and ** depicts p ≤ 0.01 wrt to control. Means denoted by the different letters within parameter are significantly different at p ≤0.05.
    C Violaceum, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/chromobacterium+subtsugae+martin+et+al/Chromobacterium+subtsugae+Martin+et+al/pmc12801156-287-1-3
    Average 96 stars, based on 1 article reviews
    c violaceum - by Bioz Stars, 2026-10
    96/100 stars
      Buy from Supplier

    Image Search Results


    (A) Structural model of P. aeruginosa RhlR, highlighting the modular architecture that defines LuxR-type receptors: an N-terminal acyl-homoserine lactone (AHL) ligand-binding domain (LBD; turquoise) and a C-terminal helix-turn-helix (HTH) DNA-binding domain (DBD; yellow). The solvent-accessible volume of the LBD ligand-binding pocket is shown in light pink to provide structural context. Structures are derived from PDB IDs 8DQ0 and 8DQ1 , and all structure images were generated using ChimeraX. (B) Panel of AHL signal molecules recognized by the cognate receptors as in panel C. C4-HSL; P. aeruginosa ; RhlR, C6-HSL; C. subtsugae ; CviR, 3OC8-HSL; A. tumefaciens ; TraR, 3OC12-HSL; LasR; 3OHC12-HSL; A. baumannii ; AbaR. (C) Multiple sequence alignment (MSA) of LuxR-type receptors discussed in this review, spanning residues 44–72, which correspond to a conserved portion of the LBD. Amino acids are colored by physicochemical properties (positive, negative, polar, and non-polar, as indicated). A maximum-likelihood phylogenetic tree based on full-length sequences is shown to the left of the alignment. (D) Sequence alignment of the HTH DNA binding domains (residues 198–217) from the same set of receptors shown in panel B. The phylogenetic tree is omitted for clarity. Conserved residues within the HTH motif are denoted with an asterisk.

    Journal: PLOS Pathogens

    Article Title: Expanding the LuxR-type receptor functional repertoire: Protein-protein interactions in quorum sensing regulation

    doi: 10.1371/journal.ppat.1014091

    Figure Lengend Snippet: (A) Structural model of P. aeruginosa RhlR, highlighting the modular architecture that defines LuxR-type receptors: an N-terminal acyl-homoserine lactone (AHL) ligand-binding domain (LBD; turquoise) and a C-terminal helix-turn-helix (HTH) DNA-binding domain (DBD; yellow). The solvent-accessible volume of the LBD ligand-binding pocket is shown in light pink to provide structural context. Structures are derived from PDB IDs 8DQ0 and 8DQ1 , and all structure images were generated using ChimeraX. (B) Panel of AHL signal molecules recognized by the cognate receptors as in panel C. C4-HSL; P. aeruginosa ; RhlR, C6-HSL; C. subtsugae ; CviR, 3OC8-HSL; A. tumefaciens ; TraR, 3OC12-HSL; LasR; 3OHC12-HSL; A. baumannii ; AbaR. (C) Multiple sequence alignment (MSA) of LuxR-type receptors discussed in this review, spanning residues 44–72, which correspond to a conserved portion of the LBD. Amino acids are colored by physicochemical properties (positive, negative, polar, and non-polar, as indicated). A maximum-likelihood phylogenetic tree based on full-length sequences is shown to the left of the alignment. (D) Sequence alignment of the HTH DNA binding domains (residues 198–217) from the same set of receptors shown in panel B. The phylogenetic tree is omitted for clarity. Conserved residues within the HTH motif are denoted with an asterisk.

    Article Snippet: In Chromobacterium subtsugae (formerly C. violaceum ATCC 31532), CviR activates violacein production and other virulence-associated genes in response to its cognate AHL [ ].

    Techniques: Ligand Binding Assay, Binding Assay, Solvent, Derivative Assay, Generated, Sequencing

    LuxR-type QS receptors (light-green ovals) are subject to regulation by a range of protein interaction partners (purple ovals), which modulate receptor function through distinct mechanisms. Negative regulators inhibit LuxR-type receptor function by disrupting dimerization, decreasing receptor stability, and inhibiting DNA binding. Representative examples include TraM-TraR ( A. tumefaciens ) , QscR-LasR/RhlR QteE-LasR/RhlR, Aqs1-LasR (all P.s aeruginosa ), and VioS-CviR ( C. subtsugae ). Dual or context-dependent regulators modify LuxR-type receptor activity in a promoter-, ligand-, or environmental-dependent manner. Examples include PqsE-RhlR ( P. aeruginosa ) and BlsA-AbaR ( A. baumannii ), which increase DNA binding affinity and/or transcriptional output under specific conditions. Global regulators modulate LuxR-type receptor function through transcriptional engagement or post-translational control, including RNA polymerase-mediated activation and protease-dependent receptor degradation. Created in BioRender. Paczkowski, J. (2026) https://BioRender.com/akj8r1w .

    Journal: PLOS Pathogens

    Article Title: Expanding the LuxR-type receptor functional repertoire: Protein-protein interactions in quorum sensing regulation

    doi: 10.1371/journal.ppat.1014091

    Figure Lengend Snippet: LuxR-type QS receptors (light-green ovals) are subject to regulation by a range of protein interaction partners (purple ovals), which modulate receptor function through distinct mechanisms. Negative regulators inhibit LuxR-type receptor function by disrupting dimerization, decreasing receptor stability, and inhibiting DNA binding. Representative examples include TraM-TraR ( A. tumefaciens ) , QscR-LasR/RhlR QteE-LasR/RhlR, Aqs1-LasR (all P.s aeruginosa ), and VioS-CviR ( C. subtsugae ). Dual or context-dependent regulators modify LuxR-type receptor activity in a promoter-, ligand-, or environmental-dependent manner. Examples include PqsE-RhlR ( P. aeruginosa ) and BlsA-AbaR ( A. baumannii ), which increase DNA binding affinity and/or transcriptional output under specific conditions. Global regulators modulate LuxR-type receptor function through transcriptional engagement or post-translational control, including RNA polymerase-mediated activation and protease-dependent receptor degradation. Created in BioRender. Paczkowski, J. (2026) https://BioRender.com/akj8r1w .

    Article Snippet: In Chromobacterium subtsugae (formerly C. violaceum ATCC 31532), CviR activates violacein production and other virulence-associated genes in response to its cognate AHL [ ].

    Techniques: Binding Assay, Activity Assay, Control, Activation Assay

    Quantitative determination of violacein inhibition in C. violaceum 12472 by sub-MICs of CMRE. Data is presented as mean of triplicates and bar denotes SD. Different letters above the bars indicate statistically significant differences among treatments ( p < 0.05). * depicts p ≤ 0.05 wrt to control and ** depicts p ≤ 0.01 wrt to control. Means denoted by the different letters within parameter are significantly different at p ≤0.05.

    Journal: Frontiers in Microbiology

    Article Title: Commiphora myrrha resin extract inhibits the biofilms and quorum sensing controlled virulence factors of Gram-negative foodborne bacterial pathogens

    doi: 10.3389/fmicb.2025.1668863

    Figure Lengend Snippet: Quantitative determination of violacein inhibition in C. violaceum 12472 by sub-MICs of CMRE. Data is presented as mean of triplicates and bar denotes SD. Different letters above the bars indicate statistically significant differences among treatments ( p < 0.05). * depicts p ≤ 0.05 wrt to control and ** depicts p ≤ 0.01 wrt to control. Means denoted by the different letters within parameter are significantly different at p ≤0.05.

    Article Snippet: In C. violaceum (ATCC 31532), the synthesis of violacein relies on QS, mediated by C 6 -AHL.

    Techniques: Inhibition, Control