LuxR-type DNA-binding HTH domain (original) (raw)

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In molecular biology, the LuxR-type DNA-binding HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 65 amino acids. It is present in transcription regulators of the LuxR/FixJ family of response regulators. The domain is named after Vibrio fischeri luxR, a transcriptional activator for quorum-sensing control of luminescence. LuxR-type HTH domain proteins occur in a variety of organisms. The DNA-binding HTH domain is usually located in the C-terminal region of the protein; the N-terminal region often containing an autoinducer-binding domain or a response regulatory domain. Most luxR-type regulators act as transcription activators, but some can be repressors or have a dual role for different sites. LuxR-type HTH regulators control a wide variety of activities in various biolog

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dbo:abstract In molecular biology, the LuxR-type DNA-binding HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 65 amino acids. It is present in transcription regulators of the LuxR/FixJ family of response regulators. The domain is named after Vibrio fischeri luxR, a transcriptional activator for quorum-sensing control of luminescence. LuxR-type HTH domain proteins occur in a variety of organisms. The DNA-binding HTH domain is usually located in the C-terminal region of the protein; the N-terminal region often containing an autoinducer-binding domain or a response regulatory domain. Most luxR-type regulators act as transcription activators, but some can be repressors or have a dual role for different sites. LuxR-type HTH regulators control a wide variety of activities in various biological processes. The luxR-type, DNA-binding HTH domain forms a four-helical bundle structure. The HTH motif comprises the second and third helices, known as the scaffold and recognition helix, respectively. The HTH binds DNA in the major groove, where the N-terminal part of the recognition helix makes most of the DNA contacts. The fourth helix is involved in dimerisation of gerE and traR. Signalling events by one of the four activation mechanisms described below lead to multimerisation of the regulator. The regulators bind DNA as multimers. LuxR-type HTH proteins can be activated by one of four different mechanisms: 1. Regulators which belong to a two-component sensory transduction system where the protein is activated by its phosphorylation, generally on an aspartate residue, by a transmembrane kinase. Some proteins that belong to this category are: * Rhizobiaceae fixJ (global regulator inducing expression of nitrogen-fixation genes in microaerobiosis) * Escherichia coli and Salmonella typhimurium uhpA (activates hexose phosphate transport gene uhpT) * E. coli narL and narP (activate nitrate reductase operon) * Enterobacteria rcsB (regulation of exopolysaccharide biosynthesis in enteric and plant pathogenesis) * Bordetella pertussis bvgA (virulence factor) * Bacillus subtilis comA (involved in expression of late-expressing competence genes) 2. Regulators which are activated, or in very rare cases repressed, when bound to N-acyl homoserine lactones, which are used as quorum sensing molecules in a variety of Gram-negative bacteria: * Vibrio fischeri luxR (activates bioluminescence operon) * Agrobacterium tumefaciens traR (regulation of Ti plasmid transfer) * Erwinia carotovora carR (control of carbapenem antibiotics biosynthesis) * E. carotovora expR (virulence factor for soft rot disease; activates plant tissue macerating enzyme genes) * Pseudomonas aeruginosa lasR (activates elastase gene lasB) * Erwinia chrysanthemi echR and Erwinia stewartii esaR * Pseudomonas chlororaphis phzR (positive regulator of phenazine antibiotic production) * Pseudomonas aeruginosa rhlR (activates rhlAB operon and lasB gene) * Acinetobacter baumannii abaR (activates operon for production of surfactant-like lipopeptide acinetin-505) 3. Autonomous effector domain regulators, without a regulatory domain, represented by gerE. * B. subtilis gerE (transcription activator and repressor for the regulation of spore formation) 4. Multiple ligand-binding regulators, exemplified by malT. * E. coli malT (activates maltose operon; MalT binds ATP and maltotriose) (en)
dbo:symbol GerE
dbo:thumbnail wiki-commons:Special:FilePath/PDB_1p4w_EBI.jpg?width=300
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dbo:wikiPageWikiLink dbr:Proteins dbr:Elastase dbr:Molecule dbr:C-terminal dbr:Bordetella_pertussis dbr:Antibiotic dbr:Rhizobiaceae dbr:DNA dbr:N-Acyl_homoserine_lactone dbr:Ligand_(biochemistry) dbr:Gene_expression dbr:Pseudomonas_aeruginosa dbr:Enzyme dbr:Gene dbr:Genes dbr:Operon dbr:Maltose dbr:Maltotriose dbr:Spore dbr:Transcriptional_regulation dbr:Helix dbr:Erwinia_chrysanthemi dbr:Nitrate_reductase dbr:Adenosine_triphosphate dbr:Agrobacterium_tumefaciens dbr:Amino_acids dbr:Escherichia_coli dbr:Carbapenem dbr:Gram-negative_bacteria dbr:Enteric dbr:Kinase dbr:Protein_dimer dbr:Protein_domain dbr:Protein dbr:Quorum_sensing dbr:Regulation dbc:Protein_domains dbr:Helix-turn-helix dbr:Hexose dbr:Bacillus_subtilis dbr:Acinetobacter_baumannii dbr:Bioluminescence dbr:Biosynthesis dbr:Effector_(biology) dbr:Tissue_(biology) dbr:Transport dbr:Pathogenesis dbr:Pseudomonas_chlororaphis dbr:Autoinducer dbr:Phenazine dbr:Plant dbr:Enterobacteria dbr:Organism dbr:Molecular_binding dbr:Luminescence dbr:Cell_signalling dbr:Plasmid dbr:Phosphorylation dbr:Virulence_factor dbr:Repressor dbr:Quorum-sensing dbr:Vibrio_fischeri dbr:Protein_motif dbr:Salmonella_typhimurium dbr:Transcription_activators dbr:Transcriptional_activator dbr:Transmembrane dbr:Exopolysaccharide dbr:Secondary_structure dbr:Aspartate dbr:Alpha_helical dbr:N-terminal dbr:Erwinia_carotovora dbr:Erwinia_stewartii dbr:Competence_(biology) dbr:Sensory_transduction dbr:Expression_(genetics) dbr:Multimeric_protein dbr:Nitrogen-fixation
dbp:caption solution structure of the dna-binding domain of the erwinia amylovora rcsb protein (en)
dbp:interpro IPR000792 (en)
dbp:name Bacterial regulatory proteins, luxR family (en)
dbp:pfam PF00196 (en)
dbp:pfamClan CL0123 (en)
dbp:prosite PDOC00542 (en)
dbp:scop 1 (xsd:integer)
dbp:symbol GerE (en)
dbp:wikiPageUsesTemplate dbt:Infobox_protein_family dbt:InterPro_content dbt:Reflist
dct:subject dbc:Protein_domains
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rdfs:comment In molecular biology, the LuxR-type DNA-binding HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 65 amino acids. It is present in transcription regulators of the LuxR/FixJ family of response regulators. The domain is named after Vibrio fischeri luxR, a transcriptional activator for quorum-sensing control of luminescence. LuxR-type HTH domain proteins occur in a variety of organisms. The DNA-binding HTH domain is usually located in the C-terminal region of the protein; the N-terminal region often containing an autoinducer-binding domain or a response regulatory domain. Most luxR-type regulators act as transcription activators, but some can be repressors or have a dual role for different sites. LuxR-type HTH regulators control a wide variety of activities in various biolog (en)
rdfs:label LuxR-type DNA-binding HTH domain (en)
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foaf:depiction wiki-commons:Special:FilePath/PDB_1p4w_EBI.jpg
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