Category:Complex:MCP-II
About
Description (originally from EcoCyc[1][2]) MCP-II
Comments (originally from EcoCyc[1][2]) The tar gene product is one of four methyl-accepting chemotaxis proteins (MCPs) in E. coli. MCP-II is the receptor for the attractant L-aspartate and related amino acids and dicarboxylic acids. MCP-II also interacts with the periplasmic maltose-binding protein to mediate taxis to the attractant maltose. It also responds to the repellents cobalt and nickel and is thermosensitive. [3][4][5][6][7][8][9][10][11][12][13][14][15][16][9][17][18][10][19][20][21].
References
- ↑ 1.0 1.1 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 2.0 2.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ Nara, T et al. (1996) Modulation of the thermosensing profile of the Escherichia coli aspartate receptor tar by covalent modification of its methyl-accepting sites. J. Biol. Chem. 271 17932-6 PubMed
- ↑ Gardina, PJ et al. (1997) Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor. Mol. Microbiol. 23 1181-91 PubMed
- ↑ Gardina, P et al. (1992) Aspartate and maltose-binding protein interact with adjacent sites in the Tar chemotactic signal transducer of Escherichia coli. J. Bacteriol. 174 1528-36 PubMed
- ↑ Krikos, A et al. (1983) Sensory transducers of E. coli are composed of discrete structural and functional domains. Cell 33 615-22 PubMed
- ↑ Wang, EA & Koshland, DE Jr (1980) Receptor structure in the bacterial sensing system. Proc. Natl. Acad. Sci. U.S.A. 77 7157-61 PubMed
- ↑ Chi, YI et al. (1997) Apo structure of the ligand-binding domain of aspartate receptor from Escherichia coli and its comparison with ligand-bound or pseudoligand-bound structures. FEBS Lett. 414 327-32 PubMed
- ↑ 9.0 9.1 Manson, MD et al. (1998) Bacterial locomotion and signal transduction. J. Bacteriol. 180 1009-22 PubMed
- ↑ 10.0 10.1 Falke, JJ et al. (1997) The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes. Annu. Rev. Cell Dev. Biol. 13 457-512 PubMed
- ↑ Gegner, JA et al. (1992) Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway. Cell 70 975-82 PubMed
- ↑ Shimizu, TS et al. (2000) Molecular model of a lattice of signalling proteins involved in bacterial chemotaxis. Nat. Cell Biol. 2 792-6 PubMed
- ↑ Bren, A & Eisenbach, M (2000) How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation. J. Bacteriol. 182 6865-73 PubMed
- ↑ Welch, M et al. (1993) Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proc. Natl. Acad. Sci. U.S.A. 90 8787-91 PubMed
- ↑ Barak, R & Eisenbach, M (1992) Correlation between phosphorylation of the chemotaxis protein CheY and its activity at the flagellar motor. Biochemistry 31 1821-6 PubMed
- ↑ Hess, JF et al. (1987) Protein phosphorylation is involved in bacterial chemotaxis. Proc. Natl. Acad. Sci. U.S.A. 84 7609-13 PubMed
- ↑ Yeh, JI et al. (1993) The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding. J. Biol. Chem. 268 9787-92 PubMed
- ↑ Toews, ML et al. (1979) Attractants and repellents control demethylation of methylated chemotaxis proteins in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 76 5544-8 PubMed
- ↑ Sourjik, V & Berg, HC (2000) Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions. Mol. Microbiol. 37 740-51 PubMed
- ↑ Borkovich, KA et al. (1992) Attenuation of sensory receptor signaling by covalent modification. Proc. Natl. Acad. Sci. U.S.A. 89 6756-60 PubMed
- ↑ Li, G & Weis, RM (2000) Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli. Cell 100 357-65 PubMed
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