Signal transduction: Hair brains in bacterial chemotaxis

Current Biology

Volumn 10, Issue 1, 2000, Pages

  Stock, Jeff ^a   Levit, Mikhail ^a  

^a PRINCETON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0033957812     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)00248-1     Document Type: Review

References (30)

1. Yeh J.I., Biemann H.P., Prive G.G., Pandit J., Koshland D.E. Jr., Kim S.H. High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor. J Mol Biol. 262:1996;186-201.
2. Falke J.J., Bass R.B., Butler S.L., Chervitz S.A., Danielson M.A. 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. 13:1997;457-512.
3. Kim K.K., Yokota H., Kim S.H. Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor. Nature. 400:1999;787-792.
4. Surette M.G., Stock J.B. Role of alpha-helical coiled-coil interactions in receptor dimerization, signaling, and adaptation during bacterial chemotaxis. J Biol Chem. 271:1996;17966-17973.
5. Ames P., Yu Y.A., Parkinson J.S. Methylation segments are not required for chemotactic signalling by cytoplasmic fragments of Tsr, the methyl-accepting serine chemoreceptor of Escherichia coli. Mol Microbiol. 19:1996;737-746.
6. Rudolph J., Nordmann B., Storch K.F., Gruenberg H., Rodewald K., Oesterhelt D. A family of halobacterial transducer proteins. FEMS Microbiol Lett. 139:1996;161-168.
7. Le Moual H., Koshland D.E. Jr. Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis. J Mol Biol. 261:1996;568-585.
8. Bilwes A.M., Alex L.A., Crane B.R., Simon M.I. Structure of CheA, a signal-transducing histidine kinase. Cell. 96:1999;131-141.
9. Stock J. Signal transduction: Gyrating protein kinases. Curr Biol. 9:1999;R364-R367.
10. Morrison T.B., Parkinson J.S. Liberation of an interaction domain from the phosphotransfer region of CheA, a signaling kinase of Escherichia coli. Proc Natl Acad Sci USA. 91:1994;5485-5489.
11. Zhou H., McEvoy M.M., Lowry D.F., Swanson R.V., Simon M.I., Dahlquist F.W. Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker. Biochemistry. 35:1996;433-443.
12. Zhou H., Lowry D.F., Swanson R.V., Simon M.I., Dahlquist F.W. NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics. Biochemistry. 34:1995;13858-13870.
13. Grebe T.W., Stock J.B. The histidine protein kinase superfamily. Adv Microb Physiol. 41:1999;139-227.
14. McEvoy M.M., Hausrath A.C., Randolph G.B., Remington S.J., Dahlquist F.W. Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway. Proc Natl Acad Sci USA. 95:1998;7333-7338.
15. Welch M., Chinardet N., Mourey L., Birck C., Samama J.P. Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY. Nat Struct Biol. 5:1998;25-29.
16. Schuster S.C., Swanson R.V., Alex L.A., Bourret R.B., Simon M.I. Assembly and function of a quaternary signal transduction complex monitored by surface plasmon resonance. Nature. 365:1993;343-347.
17. Scharf B.E., Fahrner K.A., Turner L., Berg H.C. Control of direction of flagellar rotation in bacterial chemotaxis. Proc Natl Acad Sci USA. 95:1998;201-206.
18. Alon U., Camarena L., Surette M.G., Aguera y Arcas B., Liu Y., Liebler S., Stock J.B. Response regulator output in bacterial chemotaxis. EMBO J. 17:1998;4238-4248.
19. Chi Y.I., Yokota H., Kim S.H. 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. 414:1997;327-332.
20. Biemann H.P., Koshland D.E. Jr. Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativity. Biochemistry. 33:1994;629-634.
21. Chervitz S.A., Falke J.J. Molecular mechanism of transmembrane signaling by the aspartate receptor: a model. Proc Natl Acad Sci USA. 93:1996;2545-2550.
22. Ottemann K.M., Xiao W., Shin Y.K., Koshland D.E. Jr. A piston model for transmembrane signaling of the aspartate receptor. Science. 285:1999;1751-1754.
23. Maddock J.R., Shapiro L. Polar location of the chemoreceptor complex in the Escherichia coli cell. Science. 259:1993;1717-1723.
24. Liu Y., Levit M., Lurz R., Surette M., Stock J. Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis. EMBO J. 16:1997;7231-7240.
25. Stock, J., Da Re, S.: A receptor scaffold mediates stimulus-response coupling in bacterial chemotaxis. Cell Calcium 1999, in press.
26. Djordjevic S., Goudreau P.N., Xu Q., Stock A.M., West A.H. Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain. Proc Natl Acad Sci USA. 95:1998;1381-1386.
27. Stock J.B., Surette M. Chemotaxis. Neidhardt F.C. Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. 1996;1103-1129 ASM, Washington, DC.
28. Djordjevic S., Stock A.M. Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. Structure. 5:1997;545-558.
29. Grebe T.W., Stock J. Bacterial chemotaxis: The five sensors of a bacterium. Curr Biol. 8:1998;R154-R157.
30. Stock J., Stock A. What is the role of receptor methylation in bacterial chemotaxis? Trends Biochemical Sci. 12:1987;371-375.