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Members of the IclR family of bacterial transcriptional regulators function as activators and/or repressors.
FEMS Microbiol Rev. 2006 Mar; 30(2):157-86.FM

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.

Authors+Show Affiliations

Consejo Superior de Investigaciones Científicas, Estación Experimental del Zaidín, Department of Biochemistry and Molecular and Cellular Biology of Plants, Granada, Spain.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

16472303

Citation

Molina-Henares, Antonio J., et al. "Members of the IclR Family of Bacterial Transcriptional Regulators Function as Activators And/or Repressors." FEMS Microbiology Reviews, vol. 30, no. 2, 2006, pp. 157-86.
Molina-Henares AJ, Krell T, Eugenia Guazzaroni M, et al. Members of the IclR family of bacterial transcriptional regulators function as activators and/or repressors. FEMS Microbiol Rev. 2006;30(2):157-86.
Molina-Henares, A. J., Krell, T., Eugenia Guazzaroni, M., Segura, A., & Ramos, J. L. (2006). Members of the IclR family of bacterial transcriptional regulators function as activators and/or repressors. FEMS Microbiology Reviews, 30(2), 157-86.
Molina-Henares AJ, et al. Members of the IclR Family of Bacterial Transcriptional Regulators Function as Activators And/or Repressors. FEMS Microbiol Rev. 2006;30(2):157-86. PubMed PMID: 16472303.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Members of the IclR family of bacterial transcriptional regulators function as activators and/or repressors. AU - Molina-Henares,Antonio J, AU - Krell,Tino, AU - Eugenia Guazzaroni,Maria, AU - Segura,Ana, AU - Ramos,Juan L, PY - 2006/2/14/pubmed PY - 2006/4/28/medline PY - 2006/2/14/entrez SP - 157 EP - 86 JF - FEMS microbiology reviews JO - FEMS Microbiol Rev VL - 30 IS - 2 N2 - 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. SN - 0168-6445 UR - https://www.unboundmedicine.com/medline/citation/16472303/Members_of_the_IclR_family_of_bacterial_transcriptional_regulators_function_as_activators_and/or_repressors_ L2 - https://academic.oup.com/femsre/article-lookup/doi/10.1111/j.1574-6976.2005.00008.x DB - PRIME DP - Unbound Medicine ER -