Probing the nucleotide binding and phosphorylation by the histidine kinase of a novel three-protein two-component system from Mycobacterium tuberculosis

FEBS Letters

Volumn 581, Issue 9, 2007, Pages 1903-1909

  Shrivastava, Rashmi ^a   Ghosh, Ananta Kumar ^a   Das, Amit Kumar ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY   (India)

Author keywords

ATP binding; ATPase assay; Fluorescence; Phosphotransfer; Response regulator; TNP ATP

Indexed keywords

PROTEIN HISTIDINE KINASE;

ARTICLE; ENZYME PHOSPHORYLATION; GENE SEQUENCE; MOLECULAR PROBE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUCLEOTIDE BINDING SITE; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN INTERACTION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STOICHIOMETRY;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; DNA-BINDING PROTEINS; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; MYCOBACTERIUM TUBERCULOSIS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN KINASES; SEQUENCE HOMOLOGY, AMINO ACID;

MYCOBACTERIUM TUBERCULOSIS;

EID: 34247170877     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.03.089     Document Type: Article

References (24)

1. Stock A.M., Wylie D.C., Mottonen J.M., Lupas A.N., Ninfa E.G., Ninfa A.J., Schutt C.E., and Stock J.B. Phosphoproteins involved in bacterial signal transduction. Cold Spring Harb. Symp. Quant. Biol. 53 (1988) 49-57
2. Bilwes A.M., Alex L.A., Crane B.R., and Simon M.I. Structure of CheA, a signal-transducing histidine kinase. Cell 96 (1999) 131-141
3. Cai S.J., Khorchid A., Ikura M., and Inouye M. Probing catalytically essential domain orientation in histidine kinase EnvZ by targeted disulfide crosslinking. J. Mol. Biol. 328 (2003) 409-418
4. Blue C.E., and Mitchell T.J. Contribution of a response regulator to the virulence of Streptococcus pneumoniae is strain dependent. Infect. Immun. 71 (2003) 4405-4413
5. Dziejman M., and Mekalanos J.J. Two-component signal transduction and its role in the expression of bacterial virulence factors. In: Hoch J.A., and Silhavy T.J. (Eds). Two-component Signal Transduction (1995), ASM Press, Washington, DC 305-317
6. Perez E., Samper S., Bordas Y., Guilhot C., Gicquel B., and Martin C. An essential role for PhoP in Mycobacterium tuberculosis virulence. Mol. Microbiol. 41 (2001) 179-187
7. Loomis W.F., Shaulsky G., and Wang N. Histidine kinases in signal transduction pathways of eukaryotes. J. Cell Sci. 110 (1997) 1141-1145
8. Stephenson K., and Hoch J.A. Developing inhibitors to selectively target two-component and phosphorelay signal transduction systems of pathogenic microorganisms. Curr. Med. Chem. 11 (2004) 765-773
9. Grebe T.W., and Stock J.B. The histidine protein kinase superfamily. Adv. Microb. Physiol 41 (1999) 139-227
10. Tanaka T., Saha S.K., Tomomori C., Ishima R., Liu D., Tong K.I., Park H., Dutta R., Qin L., Swindells M.B., Yamazaki T., Ono A.M., Kainosho M., Inouye M., and Ikura M. NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ. Nature 396 (1998) 88-92
11. Bilwes A.M., Quezada C.M., Croal L.R., Crane B.R., and Simon M.I. Nucleotide binding by the histidine kinase CheA. Nat. Struct. Biol. 8 (2001) 353-360
12. Plesniak L., Horiuchi Y., Sem D., Meinenger D., Stiles L., Shaffer J., Jennings P.A., and Adams J.A. Probing the nucleotide binding domain of the osmoregulator EnvZ using fluorescent nucleotide derivatives. Biochemistry 41 (2002) 13876-13882
13. Stewart R.C., VanBruggen R., Ellefson D.D., and Wolfe A.J. TNP-ATP and TNP-ADP as probes of the nucleotide binding site of CheA, the histidine protein kinase in the chemotaxis signal transduction pathway of Escherichia coli. Biochemistry 37 (1998) 12269-12279
14. Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., Gordon S.V., Eiglmeier K., Gas S., Barry III C.E., Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., and Barrell B.G. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 (1998) 537-544
15. Waddell S.J., Stabler R.A., Laing K., Kremer L., Reynolds R.C., and Besra G.S. The use of microarray analysis to determine the gene expression profiles of Mycobacterium tuberculosis in response to anti-bacterial compounds. Tuberculosis 84 (2004) 263-274
16. Shrivastava R., Das D.R., Wiker H.G., and Das A.K. Functional insights from the molecular modelling of a novel two-component system. Biochem. Biophys. Res. Commun. 344 (2006) 1327-1333
17. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acid Res. 22 (1994) 4673-4680
18. Clamp M., Cuff J., Searle S.M., and Barton G.J. The Jalview Java alignment editor. Bioinformatics 12 (2004) 426-427
19. Taira K., and Benkovic S.J. Evaluation of the importance of hydrophobic interactions in drug binding to dihydrofolate reductase. J. Med. Chem. 31 (1988) 129-137
20. Dixon M., and Webb E.C. Enzymes (1979), Longman Group, London
21. Penefsky H.S., and Bruist M.F. Adenosinetriphosphatases. In: Bergmeyer H.U. (Ed). Methods of Enzymatic Analysis (1984), Verlag chemie, Weinheim 324-325
22. Janiak-Spens F., Sparling D.P., and West A.H. Novel role for an HPt domain in stabilizing the phosphorylated state of a response regulator domain. J. Bacteriol. 182 (2000) 6673-6678
23. Xu Q., Porter S.W., and West A.H. The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems. Structure 11 (2003) 1569-1581
24. Ishige K., Nagasawa S., Tokishita S.-I., and Mizuno T. A novel device of bacterial signal transducers. EMBO J. 13 (1994) 5195-5202