rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2000-10-27
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pubmed:abstractText |
Iron is essential for all organisms but can be toxic in excess. Iron homeostasis is typically regulated by cytoplasmic iron binding proteins, but here we describe a signal transduction system (PmrA/PmrB) that responds to extracytoplasmic ferric iron. Iron promoted transcription of PmrA-activated genes and resistance to the antibiotic polymyxin in Salmonella. The PmrB protein bound iron via its periplasmic domain which harbors two copies of the sequence ExxE, a motif present in the Saccharomyces FTR1 iron transporter and in mammalian ferritin light chain. A pmrA mutant was hypersensitive to killing by iron but displayed wild-type resistance to a variety of oxidants, suggesting PmrA/PmrB controls a novel pathway mediating the avoidance of iron toxicity.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Iron-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PhoP protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/PhoQ protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/PmrB protein, bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Polymyxins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Transferrin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/pmrA protein, Bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
103
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
113-25
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11051552-Bacterial Proteins,
pubmed-meshheading:11051552-Binding Sites,
pubmed-meshheading:11051552-Carrier Proteins,
pubmed-meshheading:11051552-Drug Resistance, Microbial,
pubmed-meshheading:11051552-Extracellular Space,
pubmed-meshheading:11051552-Gene Expression Regulation, Bacterial,
pubmed-meshheading:11051552-Iron,
pubmed-meshheading:11051552-Iron-Binding Proteins,
pubmed-meshheading:11051552-Phenotype,
pubmed-meshheading:11051552-Polymyxins,
pubmed-meshheading:11051552-Protein Structure, Tertiary,
pubmed-meshheading:11051552-Salmonella enterica,
pubmed-meshheading:11051552-Signal Transduction,
pubmed-meshheading:11051552-Transcription, Genetic,
pubmed-meshheading:11051552-Transcription Factors,
pubmed-meshheading:11051552-Transferrin-Binding Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
A signal transduction system that responds to extracellular iron.
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pubmed:affiliation |
Department of Molecular Microbiology, Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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