Members of the IclR family of bacterial transcriptional regulators function as activators and/or repressors

Abstract Members of the IclR family of regulators are proteins with around 250 residues. The IclR family is best defined by a profile covering the effector binding domain. This is supported by structural data and by a number of mutants showing that effector specificity lies within a pocket in the C-...

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Published inFEMS microbiology reviews Vol. 30; no. 2; pp. 157 - 186
Main Authors Molina-Henares, Antonio J., Krell, Tino, Eugenia Guazzaroni, Maria, Segura, Ana, Ramos, Juan L.
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 01.03.2006
Blackwell Science Ltd
Oxford University Press
Subjects
Amino Acid Sequence
Aromatic compounds
Bacterial Proteins - chemistry
Bacterial Proteins - physiology
Binding sites
Biodegradation
catabolic pathways
Cyclic AMP Receptor Protein - physiology
Databases, Genetic
Deactivation
Deoxyribonucleic acid
Dimers
DNA
DNA-directed RNA polymerase
Erwinia - pathogenicity
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Escherichia coli Proteins - physiology
Gene Expression Regulation, Bacterial - genetics
Glyoxylates - metabolism
Helix-Turn-Helix Motifs - genetics
IclR family
Inactivation
Krebs cycle control
Molecular Sequence Data
Multidrug resistance
Mutants
Pathogenicity
Pathogens
profiles
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Regulators
Repressor Proteins - chemistry
Repressor Proteins - genetics
Repressor Proteins - physiology
Repressors
Ribonucleic acid
RNA
RNA polymerase
Sequence Homology, Amino Acid
Shunt resistance
solvent efflux pumps
Sporulation
Streptomyces - genetics
Streptomyces - physiology
Thermotoga maritima - genetics
Transcription
Transcription Factors - chemistry
Transcription Factors - genetics
Transcription Factors - physiology
IclR family
profiles
solvent efflux pumps
Krebs cycle control
catabolic pathways
sporulation
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Abstract Abstract Members of the IclR family of regulators are proteins with around 250 residues. The IclR family is best defined by a profile covering the effector binding domain. This is supported by structural data and by a number of mutants showing that effector specificity lies within a pocket in the C-terminal domain. These regulators have a helix-turn-helix DNA binding motif in the N-terminal domain and bind target promoters as dimers or as a dimer of dimers. This family comprises regulators acting as repressors, activators and proteins with a dual role. Members of the IclR family control genes whose products are involved in the glyoxylate shunt in Enterobacteriaceae , multidrug resistance, degradation of aromatics, inactivation of quorum-sensing signals, determinants of plant pathogenicity and sporulation. No clear consensus exists on the architecture of DNA binding sites for IclR activators: the MhpR binding site is formed by a 15-bp palindrome, but the binding sites of PcaU and PobR are three perfect 10-bp sequence repetitions forming an inverted and a direct repeat. IclR-type positive regulators bind their promoter DNA in the absence of effector. The mechanism of repression differs among IclR-type regulators. In most of them the binding sites of RNA polymerase and the repressor overlap, so that the repressor occludes RNA polymerase binding. In other cases the repressor binding site is distal to the RNA polymerase, so that the repressor destabilizes the open complex.
AbstractList Members of the IclR family of regulators are proteins with around 250 residues. The IclR family is best defined by a profile covering the effector binding domain. This is supported by structural data and by a number of mutants showing that effector specificity lies within a pocket in the C-terminal domain. These regulators have a helix-turn-helix DNA binding motif in the N-terminal domain and bind target promoters as dimers or as a dimer of dimers. This family comprises regulators acting as repressors, activators and proteins with a dual role. Members of the IclR family control genes whose products are involved in the glyoxylate shunt in Enterobacteriaceae, multidrug resistance, degradation of aromatics, inactivation of quorum-sensing signals, determinants of plant pathogenicity and sporulation. No clear consensus exists on the architecture of DNA binding sites for IclR activators: the MhpR binding site is formed by a 15-bp palindrome, but the binding sites of PcaU and PobR are three perfect 10-bp sequence repetitions forming an inverted and a direct repeat. IclR-type positive regulators bind their promoter DNA in the absence of effector. The mechanism of repression differs among IclR-type regulators. In most of them the binding sites of RNA polymerase and the repressor overlap, so that the repressor occludes RNA polymerase binding. In other cases the repressor binding site is distal to the RNA polymerase, so that the repressor destabilizes the open complex.
Abstract Members of the IclR family of regulators are proteins with around 250 residues. The IclR family is best defined by a profile covering the effector binding domain. This is supported by structural data and by a number of mutants showing that effector specificity lies within a pocket in the C-terminal domain. These regulators have a helix-turn-helix DNA binding motif in the N-terminal domain and bind target promoters as dimers or as a dimer of dimers. This family comprises regulators acting as repressors, activators and proteins with a dual role. Members of the IclR family control genes whose products are involved in the glyoxylate shunt in Enterobacteriaceae , multidrug resistance, degradation of aromatics, inactivation of quorum-sensing signals, determinants of plant pathogenicity and sporulation. No clear consensus exists on the architecture of DNA binding sites for IclR activators: the MhpR binding site is formed by a 15-bp palindrome, but the binding sites of PcaU and PobR are three perfect 10-bp sequence repetitions forming an inverted and a direct repeat. IclR-type positive regulators bind their promoter DNA in the absence of effector. The mechanism of repression differs among IclR-type regulators. In most of them the binding sites of RNA polymerase and the repressor overlap, so that the repressor occludes RNA polymerase binding. In other cases the repressor binding site is distal to the RNA polymerase, so that the repressor destabilizes the open complex.
Author Segura, Ana
Molina-Henares, Antonio J.
Eugenia Guazzaroni, Maria
Krell, Tino
Ramos, Juan L.
Author_xml – sequence: 1
  givenname: Antonio J.
  surname: Molina-Henares
  fullname: Molina-Henares, Antonio J.
  organization: Consejo Superior de Investigaciones Científicas, Estación Experimental del Zaidín, Department of Biochemistry and Molecular and Cellular Biology of Plants, Granada, Spain
– sequence: 2
  givenname: Tino
  surname: Krell
  fullname: Krell, Tino
  organization: Consejo Superior de Investigaciones Científicas, Estación Experimental del Zaidín, Department of Biochemistry and Molecular and Cellular Biology of Plants, Granada, Spain
– sequence: 3
  givenname: Maria
  surname: Eugenia Guazzaroni
  fullname: Eugenia Guazzaroni, Maria
  organization: Consejo Superior de Investigaciones Científicas, Estación Experimental del Zaidín, Department of Biochemistry and Molecular and Cellular Biology of Plants, Granada, Spain
– sequence: 4
  givenname: Ana
  surname: Segura
  fullname: Segura, Ana
  organization: Consejo Superior de Investigaciones Científicas, Estación Experimental del Zaidín, Department of Biochemistry and Molecular and Cellular Biology of Plants, Granada, Spain
– sequence: 5
  givenname: Juan L.
  surname: Ramos
  fullname: Ramos, Juan L.
  email: jlramos@eez.csic.es
  organization: Consejo Superior de Investigaciones Científicas, Estación Experimental del Zaidín, Department of Biochemistry and Molecular and Cellular Biology of Plants, Granada, Spain
BackLink https://www.ncbi.nlm.nih.gov/pubmed/16472303$$D View this record in MEDLINE/PubMed
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Keywords IclR family
profiles
solvent efflux pumps
Krebs cycle control
catabolic pathways
sporulation
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Snippet Abstract Members of the IclR family of regulators are proteins with around 250 residues. The IclR family is best defined by a profile covering the effector...
Members of the IclR family of regulators are proteins with around 250 residues. The IclR family is best defined by a profile covering the effector binding...
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StartPage 157
SubjectTerms Amino Acid Sequence
Aromatic compounds
Bacterial Proteins - chemistry
Bacterial Proteins - physiology
Binding sites
Biodegradation
catabolic pathways
Cyclic AMP Receptor Protein - physiology
Databases, Genetic
Deactivation
Deoxyribonucleic acid
Dimers
DNA
DNA-directed RNA polymerase
Erwinia - pathogenicity
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Escherichia coli Proteins - physiology
Gene Expression Regulation, Bacterial - genetics
Glyoxylates - metabolism
Helix-Turn-Helix Motifs - genetics
IclR family
Inactivation
Krebs cycle control
Molecular Sequence Data
Multidrug resistance
Mutants
Pathogenicity
Pathogens
profiles
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Regulators
Repressor Proteins - chemistry
Repressor Proteins - genetics
Repressor Proteins - physiology
Repressors
Ribonucleic acid
RNA
RNA polymerase
Sequence Homology, Amino Acid
Shunt resistance
solvent efflux pumps
Sporulation
Streptomyces - genetics
Streptomyces - physiology
Thermotoga maritima - genetics
Transcription
Transcription Factors - chemistry
Transcription Factors - genetics
Transcription Factors - physiology
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Title Members of the IclR family of bacterial transcriptional regulators function as activators and/or repressors
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