Source:http://linkedlifedata.com/resource/pubmed/id/12829265
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
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pubmed:dateCreated |
2003-6-27
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pubmed:abstractText |
The MerR family is a group of transcriptional activators with similar N-terminal helix-turn-helix DNA binding regions and C-terminal effector binding regions that are specific to the effector recognised. The signature of the family is amino acid similarity in the first 100 amino acids, including a helix-turn-helix motif followed by a coiled-coil region. With increasing recognition of members of this class over the last decade, particularly with the advent of rapid bacterial genome sequencing, MerR-like regulators have been found in a wide range of bacterial genera, but not yet in archaea or eukaryotes. The few MerR-like regulators that have been studied experimentally have been shown to activate suboptimal sigma(70)-dependent promoters, in which the spacing between the -35 and -10 elements recognised by the sigma factor is greater than the optimal 17+/-1 bp. Activation of transcription is through protein-dependent DNA distortion. The majority of regulators in the family respond to environmental stimuli, such as oxidative stress, heavy metals or antibiotics. A subgroup of the family activates transcription in response to metal ions. This subgroup shows sequence similarity in the C-terminal effector binding region as well as in the N-terminal region, but it is not yet clear how metal discrimination occurs. This subgroup of MerR family regulators includes MerR itself and may have evolved to generate a variety of specific metal-responsive regulators by fine-tuning the sites of metal recognition.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MerR protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Metals,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0168-6445
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
145-63
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12829265-Amino Acid Sequence,
pubmed-meshheading:12829265-Bacterial Proteins,
pubmed-meshheading:12829265-DNA-Binding Proteins,
pubmed-meshheading:12829265-Evolution, Molecular,
pubmed-meshheading:12829265-Genes, Bacterial,
pubmed-meshheading:12829265-Metals,
pubmed-meshheading:12829265-Models, Genetic,
pubmed-meshheading:12829265-Molecular Sequence Data,
pubmed-meshheading:12829265-Protein Structure, Tertiary,
pubmed-meshheading:12829265-Sequence Alignment,
pubmed-meshheading:12829265-Transcription Factors
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pubmed:year |
2003
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pubmed:articleTitle |
The MerR family of transcriptional regulators.
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pubmed:affiliation |
School of Biosciences, The University of Birmingham, Edgbaston, Birmingham B15 2TT, UK. n.l.brown@bham.ac.uk
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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