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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2000-6-13
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pubmed:abstractText |
The PmrA-PmrB two-component system of Salmonella enterica controls resistance to the peptide antibiotic polymyxin B and to several antimicrobial proteins from human neutrophils. Transcription of PmrA-activated genes is induced by high iron, but can also be promoted by growth in low magnesium in a process that requires another two-component system, PhoP-PhoQ. Here, we define the genetic basis for the interaction between the PhoP-PhoQ and PmrA-PmrB systems. We have identified pmrD as a PhoP-activated gene that mediates the transcriptional activation of PmrA-regulated genes during growth in low magnesium. When transcription of pmrD is driven from a heterologous promoter, expression of PmrA-activated genes occurs even at repressing magnesium concentrations and becomes independent of the phoP and phoQ genes. The PmrD effect is specific for PmrA-regulated genes and requires functional PmrA and PmrB proteins. A pmrD mutant is sensitive to polymyxin if grown in low magnesium, but resistant if grown in high iron. The PmrD protein controls the activity of the PmrA-PmrB system at a post-transcriptional level.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-10094672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-10203840,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-10464230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-10480935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-10633113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-1551826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-1824701,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-2556636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-2558046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-2646710,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-2674945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-2985470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-3523484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-4355486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-6199303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-6345791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-7489905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-7543474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-7603411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-8206837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-8391535,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-8430070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-8548821,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-8752324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-8868347,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-8900137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-8955299,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-8955307,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-8999810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-9130712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-9191038,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-9371451,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-9489669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-9570402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10775270-9988472
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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/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/PhoP protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/PhoQ protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Polymyxins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Single-Strand Specific DNA and RNA...,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/pmrA protein, Bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1861-72
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10775270-Anti-Bacterial Agents,
pubmed-meshheading:10775270-Bacterial Proteins,
pubmed-meshheading:10775270-Base Sequence,
pubmed-meshheading:10775270-Drug Resistance, Microbial,
pubmed-meshheading:10775270-Iron,
pubmed-meshheading:10775270-Magnesium,
pubmed-meshheading:10775270-Models, Biological,
pubmed-meshheading:10775270-Molecular Sequence Data,
pubmed-meshheading:10775270-Mutagenesis,
pubmed-meshheading:10775270-Mutation,
pubmed-meshheading:10775270-Phosphorylation,
pubmed-meshheading:10775270-Plasmids,
pubmed-meshheading:10775270-Polymyxins,
pubmed-meshheading:10775270-Protein Binding,
pubmed-meshheading:10775270-RNA Processing, Post-Transcriptional,
pubmed-meshheading:10775270-Recombinant Proteins,
pubmed-meshheading:10775270-Salmonella enterica,
pubmed-meshheading:10775270-Signal Transduction,
pubmed-meshheading:10775270-Single-Strand Specific DNA and RNA Endonucleases,
pubmed-meshheading:10775270-Transcription, Genetic,
pubmed-meshheading:10775270-Transcription Factors
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pubmed:year |
2000
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pubmed:articleTitle |
A small protein that mediates the activation of a two-component system by another two-component system.
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pubmed:affiliation |
Department of Molecular Microbiology, Howard Hughes Medical Institute, Washington University School of Medicine, St Louis, MO 63110-1093, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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