Interaction between the CheY response regulator and the histidine-containing phosphotransfer (HPt) domain of the ArcB sensory kinase in Escherichia coli

FEBS Letters

Volumn 408, Issue 3, 1997, Pages 337-340

  Yaku, Hidenobu ^a   Kato, Masato ^b   Hakoshima, Toshio ^b   Tsuzuki, Masakatsu ^a   Mizuno, Takeshi ^a  

^a NAGOYA UNIVERSITY   (Japan)

^b NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

ArcB anerobic sensor; CheY response regulator; HPt phosphotransfer domain; Phosphotransfer signaling in E. coli

Indexed keywords

PHOSPHOTRANSFERASE;

ARTICLE; ESCHERICHIA COLI; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HISTIDINE; MEMBRANE PROTEINS; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; PHOSPHOTRANSFERASES; PROTEIN KINASES; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

ESCHERICHIA COLI;

EID: 0031587037     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(97)00459-6     Document Type: Article

References (18)

1. [1] J.S. Parkinson, Cell 73 (1993) 857-871.
2. [2] Hock, J.A. and Silhavy, T.J. (1995) in J.A. Hoch and T.J. Silhavy (Eds), Two-component signal transduction, American Society for Microbiology, Washington, DC.
3. [3] Stock, J.B., Surette, M.G., Levit, M. and Stock, A.M. (1995) in J.A. Hoch and T.J. Silhavy (Eds), Two-component signal transduction. American Society for Microbiology, Washington, DC, pp. 25-51.
4. [4] J.B. Stock, A.D. Ninfa, A.M. Stock, Microbiol. Rev. 53 (1989) 450-490.
5. [5] J.S. Parkinson, B.C. Kofoid, Annu. Rev. Genet. 26 (1992) 71-112.
6. [6] L.A. Alex, M.I. Simon, Trends Genet. 10 (1994) 133-139.
7. [7] K. Ishige, S. Nagosawa, S. Tokishita, T. Mizuno, EMBO J. 13 (1994) 5195-5202.
8. [8] M. Tsuzuki, K. Ishige, T. Mizuno, Mol. Microbiol. 18 (1995) 953-962.
9. [9] M.A. Uhl, J.F. Miller, EMBO J. 15 (1996) 1028-1036.
10. [10] F. Posas, S.M. Wurgler-Murphy, T. Maeda, E.A. Witten, T.C. Thai, H. Saito, Cell 86 (1996) 865-875.
11. [11] J.L. Appleby, J.S. Parkinson, R.B. Bourret, Cell 86 (1996) 845-848.
12. [12] M. Inouye, Cell 85 (1996) 13-14.
13. [13] B. Arico, J.F. Miller, C. Roy, S. Stibits, D. Monack, S. Falkow, R. Gross, R. Rappuoli, Proc. Natl. Acad. Sci. USA 86 (1989) 6671-6675.
14. [14] T. Maeda, M. Takekawa, H. Saito, Science 269 (1995) 554-558.
15. [15] M. Kato, T. Mizuno, T. Shimizu, T. Hakoshima, Cell 88 (1997) 717-723.
16. [16] S. Nagasawa, K. Ishige, T. Mizuno, Mol. Microbiol. 6 (1992) 799-806.
17. [17] H. Zhou, D.F. Lowry, R.N. Swanson, M.I. Simon, F.W. Dahlquist, Biochemistry 34 (1995) 1358-1370.
18. [18] A.M. Stock, J.M. Mottonen, J.B. Stock, C.E. Schutt, Nature 337 (1989) 745-749.