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• W261862103 abstract "Research Article1 November 1994free access A novel device of bacterial signal transducers. K. Ishige K. Ishige Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Japan. Search for more papers by this author S. Nagasawa S. Nagasawa Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Japan. Search for more papers by this author S. Tokishita S. Tokishita Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Japan. Search for more papers by this author T. Mizuno T. Mizuno Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Japan. Search for more papers by this author K. Ishige K. Ishige Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Japan. Search for more papers by this author S. Nagasawa S. Nagasawa Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Japan. Search for more papers by this author S. Tokishita S. Tokishita Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Japan. Search for more papers by this author T. Mizuno T. Mizuno Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Japan. Search for more papers by this author Author Information K. Ishige1, S. Nagasawa1, S. Tokishita1 and T. Mizuno1 1Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Japan. The EMBO Journal (1994)13:5195-5202https://doi.org/10.1002/j.1460-2075.1994.tb06850.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The osmoregulatory expression of ompC and ompF in Escherichia coli is mediated by a pair of bacterial signal transduction proteins, EnvZ (sensory kinase) and OmpR (response regulator). We isolated previously multicopy suppressors which can complement a defect in the phosphotransfer signal transduction caused by an envZ deletion mutation. Among such suppressors, arcB and barA are of particular interest because these gene products are unique in the sense that they contain both an autophosphorylated histidine site (or transmitter module) and a phospho-accepting aspartate site (or receiver module) in their primary amino acid sequences. Here we report that ArcB and BarA possess in the C-terminal region a phosphorylated histidine site which has never been noticed, in addition to the authentic one identified previously. This newly identified histidine in ArcB and BarA was demonstrated to play a crucial role in the observed multicopy suppression. Furthermore, it was demonstrated in vivo and in vitro for ArcB that the C-terminal domain containing the histidine can function as an alternative phosphodonor (or transmitter). This novel type of sensory kinase was therefore revealed to contain two independent phosphodonor sites, together with a phospho-accepting site. These findings suggest that this unique feature of ArcB and BarA, in terms of the signaling modules, make it possible for these sensory kinases to function as dual-signaling transducers. Previous ArticleNext Article Volume 13Issue 211 November 1994In this issue RelatedDetailsLoading ..." @default.
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• W261862103 title "A novel device of bacterial signal transducers." @default.
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