Linked Life Data

16472303

Source:http://linkedlifedata.com/resource/pubmed/id/16472303

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-2-13
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0168-6445
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-86
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16472303-Amino Acid Sequence, pubmed-meshheading:16472303-Bacterial Proteins, pubmed-meshheading:16472303-Cyclic AMP Receptor Protein, pubmed-meshheading:16472303-Databases, Genetic, pubmed-meshheading:16472303-Erwinia, pubmed-meshheading:16472303-Escherichia coli Proteins, pubmed-meshheading:16472303-Gene Expression Regulation, Bacterial, pubmed-meshheading:16472303-Glyoxylates, pubmed-meshheading:16472303-Helix-Turn-Helix Motifs, pubmed-meshheading:16472303-Molecular Sequence Data, pubmed-meshheading:16472303-Protein Structure, Secondary, pubmed-meshheading:16472303-Protein Structure, Tertiary, pubmed-meshheading:16472303-Repressor Proteins, pubmed-meshheading:16472303-Sequence Homology, Amino Acid, pubmed-meshheading:16472303-Streptomyces, pubmed-meshheading:16472303-Thermotoga maritima, pubmed-meshheading:16472303-Transcription Factors
pubmed:year
2006
pubmed:articleTitle
Members of the IclR family of bacterial transcriptional regulators function as activators and/or repressors.
pubmed:affiliation
Consejo Superior de Investigaciones Científicas, Estación Experimental del Zaidín, Department of Biochemistry and Molecular and Cellular Biology of Plants, Granada, Spain.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't