chromobacterium subtsugae martin et al Search Results


chromobacterium subtsugae  (ATCC)
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
chromobacterium subtsugae dsmz 17043  (DSMZ)
86
DSMZ chromobacterium subtsugae dsmz 17043
(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 Dsmz 17043, supplied by DSMZ, used in various techniques. Bioz Stars score: 86/100, 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/pmc03784491-213-22-24
Average 86 stars, based on 1 article reviews
chromobacterium subtsugae dsmz 17043 - by Bioz Stars, 2026-10
86/100 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