Abstract
IN the prokaryotic two-component signal transduction systems, recognition of an environmental stimulus by a sensor molecule results in the activation of its histidine kinase domain and phosphorylation of a histidine residue within that domain1–3. This phosphate group is then transferred to an aspartate residue in the receiver domain of a cognate response regulator molecule, resulting in the activation of its output function. Although a few eukaryotic proteins were identified recently that show sequence similarity to the prokaryotic sensors or response regulators, it has not been clear whether they constituted a part of a 'two-component' system4–7. Here we describe a two-component system in Saccharomyces cerevisiae that regulates an osmosensing MAP kinase cascade8,9.
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Parkinson, J. S. & Kofoid, E. C. A. Rev. Genet. 26, 71–112 (1992).
Stock, J. B., Lukat, G. S. & Stock, A. M. A. Rev. biophys. Chem. 20, 109–136 (1991).
Bourret, R. B., Borkovich, K. A. & Simon, M. I. A. Rev. Biochem. 60, 401–441 (1991).
Schneider-Poetsch, H. A. W., Braun, B., Marx, S. & Schaumburg, A. FEBS Lett. 281, 245–249 (1991).
Chang, C., Kwok, S. F., Bleecker, A. B. & Meyerowitz, E. M. Science 262, 539–544 (1993).
Ota, I. M. & Varshavsky, A. Science 262, 566–569 (1993).
Brown, J. L., North, S. & Bussey, H. J. Bact. 175, 6908–6915 (1993).
Boguslawski, G. & Polazzi, T. Proc. natn. Acad. Sci. U.S.A. 84, 5848–5852 (1987).
Brewster, J. L., de Valoir, T., Dwyer, N. D., Winter, E. & Gustin, M. C. Science 259, 1760–1763 (1993).
Ota, I. & Varshavsky, A. Proc. natn. Acad. Sci. U.S.A. 89, 2355–2359 (1992).
James, P., Hall, B. D., Whelen, S. & Craig, E. A. Gene 122, 101–110 (1992).
Guan, K., Deschenes, R. J. & Dixon, J. E. J. biol. Chem. 267, 10024–10030 (1992).
Maeda, T., Tsai, A. Y. M. & Saito, H. Molec. cell. Biol. 13, 5408–5417 (1993).
Boguslawski, G. J. gen. Microbiol. 138, 2425–2432 (1992).
Christianson, T. W., Sikorski, R. S., Dante, M., Shero, J. H. & Hieter, P. Gene 110, 119–122 (1992).
Sun, H., Charles, C. H., Lau, L. F. & Tonks, N. K. Cell 75, 487–493 (1993).
Ward, Y. et al. Nature 367, 651–654 (1994).
Doi, K. et al. EMBO J. 13, 61–70 (1994).
Stock, A., Koshland, D. E. J. & Stock, J. Proc. natn. Acad. Sci. U.S.A. 82, 7989–7993 (1985).
Nagasawa, S., Tokishita, S., Aiba, H. & Mizuno, T. Molec. Microbiol. 6, 799–807 (1992).
Stout, V. & Gottesman, S. J. Bact. 172, 659–669 (1990).
Alani, E., Cao, L. & Kleckner, N. Genetics 116, 541–545 (1987).
Sikorski, R. S. & Hieter, P. Genetics 122, 19–27 (1989).
Milne, G. T. & Weaver, D. T. Genes Dev. 7, 1755–1765 (1993).
Mager, W. H. & Varela, J. C. S. Molec. Microbiol. 10, 253–258 (1993).
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Maeda, T., Wurgler-Murphy, S. & Saito, H. A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature 369, 242–245 (1994). https://doi.org/10.1038/369242a0
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DOI: https://doi.org/10.1038/369242a0
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