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rdf:type |
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lifeskim:mentions |
umls-concept:C0014834,
umls-concept:C0020205,
umls-concept:C0031727,
umls-concept:C0127400,
umls-concept:C0183210,
umls-concept:C0332256,
umls-concept:C0441712,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
15
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pubmed:dateCreated |
1998-8-20
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pubmed:abstractText |
The two components ArcB and ArcA play a crucial role in the signal transduction implicated in the complex transcriptional regulatory network that allows Escherichia coli to sense various respiratory growth conditions. ArcB is a hybrid sensor kinase having multiple phosphorylation sites in its primary amino acid sequence, including a transmitter, a receiver, and a histidine-containing phosphotransfer (HPt) domain. ArcA is a DNA-binding transcriptional regulator with a receiver domain. Results of recent in vitro studies revealed multistep His-to-Asp phosphotransfer circuitry in the ArcB-ArcA signaling system. For this report we conducted a series of in vivo experiments using a set of crucial ArcB mutants to evaluate the regulation of the sdh operon. The results suggested that the phosphorylated His-717 site in the HPt domain of ArcB is essential for anaerobic repression of sdh. Nonetheless, the ArcB mutant lacking this crucial His-717 site does not necessarily exhibit a null phenotype with respect to ArcB-ArcA signaling. The HPt mutant appears to maintain an ability to signal ArcA, particularly under aerobic conditions, which results in a significant repression of sdh. Based on these and other in vivo results, we propose a model in which ArcB functions in its own right as a dual-signaling sensor that is capable of propagating two types of stimuli through two distinct phosphotransfer pathways.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-1482126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-1512197,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-1597416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-2170337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-2201868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-2964639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-7783618,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-7957084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-8001132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-8226939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-8497199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-8605872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-8808618,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-8808622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-8825099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-8892825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-9054511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-9175476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-9205844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9683496-9286997
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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 Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoenolpyruvate Sugar...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/arcA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/arcB protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
180
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3973-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9683496-Bacterial Outer Membrane Proteins,
pubmed-meshheading:9683496-Bacterial Proteins,
pubmed-meshheading:9683496-Escherichia coli,
pubmed-meshheading:9683496-Escherichia coli Proteins,
pubmed-meshheading:9683496-Gene Expression Regulation, Bacterial,
pubmed-meshheading:9683496-Histidine,
pubmed-meshheading:9683496-Membrane Proteins,
pubmed-meshheading:9683496-Mutagenesis, Site-Directed,
pubmed-meshheading:9683496-Operon,
pubmed-meshheading:9683496-Phosphoenolpyruvate Sugar Phosphotransferase System,
pubmed-meshheading:9683496-Phosphorylation,
pubmed-meshheading:9683496-Protein Kinases,
pubmed-meshheading:9683496-Protein Multimerization,
pubmed-meshheading:9683496-Recombinant Fusion Proteins,
pubmed-meshheading:9683496-Repressor Proteins,
pubmed-meshheading:9683496-Signal Transduction
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pubmed:year |
1998
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pubmed:articleTitle |
A dual-signaling mechanism mediated by the ArcB hybrid sensor kinase containing the histidine-containing phosphotransfer domain in Escherichia coli.
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pubmed:affiliation |
Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya 464-8601, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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