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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1997-2-21
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pubmed:abstractText |
Recently we demonstrated the occurrence of a novel device of signal transducers in Escherichia coli. This class of bacterial sensory kinases, typified by ArcB and BarA, possesses two phospho-donor (His) sites, together with a phospho-accepting (Asp) site. These multi-phosphorylation sites were suggested to make a phosphotransfer circuit. To clarify this complex circuitry, we carried out a series of in vitro assays involving a set of ArcB mutant proteins which have an amino acid substitution at each putative phosphorylation site (His-292, Asp-576 and His-717). By these in vitro phosphorylation and/or phosphotransfer assays, the followings were assessed: (i) ArcB autophosphorylation; (ii) ArcB-mediated phosphorylation of the cognate response regulator, ArcA; (iii) ArcB-mediated phosphorylation of its truncated form (ArcBc) encompassing only the C-terminal phosphorylation site (His-717); (iv) phosphotransfer from ArcBc to ArcA; and (v) phosphotransfer from ArcBc to ArcB. On the basis of these in vitro results, a complex circuitry was revealed for the signal transducer ArcB. This evidence obtained in vitro supports the view that ArcB can serve as a powerful device for not only propagating multi-signals, but also making up signalling networks, in ways more sophisticated than previously thought.
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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 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/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
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 |
Dec
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pubmed:issn |
0950-382X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
953-62
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8825099-Bacterial Outer Membrane Proteins,
pubmed-meshheading:8825099-Bacterial Proteins,
pubmed-meshheading:8825099-Base Sequence,
pubmed-meshheading:8825099-Binding Sites,
pubmed-meshheading:8825099-Escherichia coli,
pubmed-meshheading:8825099-Escherichia coli Proteins,
pubmed-meshheading:8825099-Membrane Proteins,
pubmed-meshheading:8825099-Molecular Sequence Data,
pubmed-meshheading:8825099-Mutagenesis, Site-Directed,
pubmed-meshheading:8825099-Oligodeoxyribonucleotides,
pubmed-meshheading:8825099-Phosphorylation,
pubmed-meshheading:8825099-Protein Kinases,
pubmed-meshheading:8825099-Repressor Proteins,
pubmed-meshheading:8825099-Signal Transduction
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pubmed:year |
1995
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pubmed:articleTitle |
Phosphotransfer circuitry of the putative multi-signal transducer, ArcB, of Escherichia coli: in vitro studies with mutants.
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pubmed:affiliation |
Laboratory of Molecular Microbiology, Nagoya University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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