Newly identified genes involved in the signal transduction of Escherichia coli K-12

Utsumi, Ryutaro; Katayama, Satoshi; Taniguchi, Manabu; Horie, Tetsuya; Ikeda, Miyoshi; Igaki, S.; Nakagawa, Hitoshi; Miwa, Akiko; Tanabe, Hiroyuki; Noda, Manjiro

doi:10.1016/0378-1119(94)90733-1

Cited by 83 publications

(73 citation statements)

References 25 publications

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“…In contrast to the cascade of protein phosphorylation and dephosphorylation events in eukaryotes using protein tyrosine or serine/threonine kinases and phosphatases, the His-Asp phosphorelay systems in bacteria efficiently and reversibly regulate gene expression or cellular locomotion. The multiple steps in eukaryotes may have evolved to impart LA Egger et al 168 Genes to Cells (1997) In the centre column, the following pairs of E. coli sensor histidine kinases and responseregulators are shown: EnvZ/OmpR (Comeau et al 1985); CpxA/CpxR (Albin et al 1986;Dong et al 1993); PhoR/PhoB (Makino et al 1986a); PhoQ/PhoP (Kasahara et al 1992); BaeS/BaeR (Nagasawa et al 1993), NarX/NarL (Egan & Stewart 1990); NarQ/NarL (Chiang et al 1992); BasS/BasR (Nagasawa et al 1993), CreC/CreB (Amemura et al 1986), KdpD/KdpE (Walderhaug et al 1992); UhpB/UhpA (Friedrich & Kadner 1987;Weston & Kadner 1988); HydH/HydG (Blattner et al 1993); NtrB/NtrC (Miranda-Rios et al 1987); EvgS/EvgA (Utsumi et al 1994); RcsS/ RcsB (Stout et al 1990); ArcB/ArcA (Drury et al 1985); BarA (Nagasawa et al 1992;Zhang & Normark 1996); and CheA/CheY (Matsumura et al 1977(Matsumura et al , 1984. The sensor histidine kinase has a conserved C-terminal kinase domain of 240 amino acids (red rectangle) which contains: the histidine residue (H) that is autophosphorylated, an asparagine, DXGXG motif, a phenylalanine, and a GXGXG motif.…”

Section: Bacterial Signal Transduction Via the Histidyl-aspartyl Phosmentioning

confidence: 99%

Signal transduction via the histidyl‐aspartyl phosphorelay

1997

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The histidyl-aspartyl phosphorelay, formerly described as the two-component system, is the predominant mode of signal transduction in bacteria. Adaptation to environmental changes occurs through a sensor histidine protein kinase and a response regulator. The histidine protein kinase is usually a transmembrane receptor and the response regulator is a cytoplasmic protein.Together the histidyl-aspartyl phosphorelay proteins mediate reversible phosphorylation events that control downstream effectors. Following autophosphorylation at a conserved histidine residue, the histidine kinase serves as a phospho-donor for the response regulator. Once phosphorylated, the response regulator mediates changes in gene expression or cellular locomotion. The EnvZ-OmpR phosphorelay system in Escherichia coli, which monitors external osmolarity and responds by differentially modulating the expression of the OmpF and OmpC major outer membrane porins, will be described as a model system. While histidine kinases were thought to be present only in prokaryotes, they have recently been identified in eukaryotic systems. Here, we review the unique and conserved features of this growing family of signal transducers.

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Section: Bacterial Signal Transduction Via the Histidyl-aspartyl Phosmentioning

confidence: 99%

Signal transduction via the histidyl‐aspartyl phosphorelay

1997

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“…Both systems show very significant sequence similarities even outside of the conserved signalling modules and, accordingly, seem to respond to similar external stimuli Utsumi et al, 1994;. Whereas the function of the Evg system is not known, the Bvg system is the master regulator of virulence in B. pertussis, the aetiological agent of whooping cough (Bordet and Gengou, 1909;Weiss and Hewlett, 1986;Scarlato et al, 1991;Gross, 1993;Uhl and Miller, 1994).…”

Section: Introductionmentioning

confidence: 99%

Specificity of the BvgAS and EvgAS phosphorelay is mediated by the C‐terminal HPt domains of the sensor proteins

Perraud

Kimmel

Weiss

et al. 1998

Molecular Microbiology

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SummaryDespite the presence of highly conserved signalling modules, significant cross-communication between different two-component systems has only rarely been observed. Domain swapping and the characterization of liberated signalling modules enabled us to characterize in vitro the protein domains that mediate specificity and are responsible for the high fidelity in the phosphorelay of the unorthodox Bvg and Evg twocomponent systems. Under equimolar conditions, significant in vitro phosphorylation of purified BvgA and EvgA proteins was only obtained by their histidine kinases, BvgS and EvgS respectively. One hybrid histidine kinase consisting of the BvgS transmitter and HPt domains and of the EvgS receiver domain (BvgS-TO-EvgS-R) was able to phosphorylate BvgA but not EvgA. In contrast, the hybrid protein consisting of the BvgS transmitter and the EvgS receiver and HPt domains (BvgS-T-EvgS-RO) was unable to phosphorylate BvgA but efficiently phosphorylated EvgA. These results demonstrate that the C-terminal HPt domains of the sensor proteins endow the unorthodox twocomponent systems with a high specificity for the corresponding regulator protein. In the case of the response regulators, the receiver but not the output domains contribute to the specific interaction with the histidine kinases, because a hybrid protein consisting of the EvgA receiver and the BvgA output domain could only be phosphorylated by the EvgS protein.

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“…Such crossregulation may be an important form of global control that links the response regulators of the two-component systems to each other or to other general regulatory systems (22). Using such cross regulation, the new two-component system of EvgS and EvgA (21) has been isolated as a multicopy suppressor of d envZ mutation, in which ompC can not be expressed. They are highly homologous to BvgS and BvgA in Bordetella pertussis.…”

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confidence: 99%

“…In B. pertussis, the etiologic agent of whooping cough, the two-component system containing BvgS and BvgA proteins positively control the pertussis toxin (ptx ), hemolysin-adenylatecyclase toxin (cya ), and filamentous hemagglutinin (fhaB) genes (3,7,13). Sequence analysis predicts that BvgA and EvgA showed almost the same size (23 kDa) and possessed an N-terminal receiver domain and a C-terminal helix-turn-helix motif (1,21). Both BvgA and EvgA are cytoplasmically located and bind to specific regions in the bvgAS (14-16) and evgAS promoters (R. Utsumi et al, unpubl.…”

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confidence: 99%