Analysis of steady-state Förster resonance energy transfer data by avoiding pitfalls: Interaction of JAK2 tyrosine kinase with N-methylanthraniloyl nucleotides

Analytical Biochemistry

Volumn 442, Issue 2, 2013, Pages 213-222

  Niranjan, Yashavanthi ^a   Ungureanu, Daniela ^a   Hammarén, Henrik ^a   Sanz Sanz, Arturo ^b   Westphal, Adrie H ^c   Borst, Jan Willem ^c   Silvennoinen, Olli ^a,d   Hilhorst, Riet ^e  

^a TAMPERE UNIVERSITY OF TECHNOLOGY   (Finland)

^b ERASMUS MEDICAL CENTER   (Netherlands)

^c WAGENINGEN UNIVERSITY   (Netherlands)

^d TAMPERE UNIVERSITY HOSPITAL   (Finland)

^e PamGene International BV   (Netherlands)

Author keywords

FRET; JAK2; Ligand binding; MANT nucleotide; Primary inner filter effect; Secondary inner filter effect

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; DISSOCIATION; ENERGY TRANSFER; ENZYMES; FORSTER RESONANCE ENERGY TRANSFER; NUCLEOTIDES;

ADENOSINE DIPHOSPHATE; ADENOSINE MONOPHOSPHATE; FRET; INNER FILTER EFFECTS; JAK2; LIGAND BINDING; NUCLEOTIDE-BINDING PROTEINS; RESONANCE ENERGY TRANSFER;

BINDING ENERGY;

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; JANUS KINASE 2; NUCLEOTIDE DERIVATIVE; 3' O (N METHYLANTHRANILOYL) ATP; 3'-O-(N-METHYLANTHRANILOYL) ATP; ANTHRANILIC ACID DERIVATIVE; DRUG DERIVATIVE; TRYPTOPHAN; TYROSINE;

ARTICLE; BINDING SITE; CONTROLLED STUDY; ENZYME BINDING; FILTER; FLUORESCENCE RESONANCE ENERGY TRANSFER; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN INTERACTION; STEADY STATE; TITRIMETRY; CHEMISTRY; FRET; HUMAN; JAK2; LIGAND BINDING; MANT NUCLEOTIDE; METABOLISM; METHODOLOGY; PRIMARY INNER FILTER EFFECT; PROTEIN BINDING; SECONDARY INNER FILTER EFFECT;

FRET; JAK2; LIGAND BINDING; MANT NUCLEOTIDE; PRIMARY INNER FILTER EFFECT; SECONDARY INNER FILTER EFFECT;

ADENOSINE TRIPHOSPHATE; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; JANUS KINASE 2; ORTHO-AMINOBENZOATES; PROTEIN BINDING; TRYPTOPHAN; TYROSINE;

EID: 84884905498     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2013.07.020     Document Type: Article

References (31)

1. D.M. Jameson, and J.F. Eccleston Fluorescent nucleotide analogs: synthesis and applications Methods Enzymol. 278 1997 363 390 (Pubitemid 27229929)
2. C.R. Bagshaw ATP analogues at a glance J. Cell. Sci. 114 2001 459 460 (Pubitemid 32186104)
3. T. Hiratsuka Fluorescent and colored trinitrophenylated analogs of ATP and GTP Eur. J. Biochem. 270 2003 3479 3485 (Pubitemid 37046729)
4. D.Q. Ni, J. Shaffer, and J.A. Adams Insights into nucleotide binding in protein kinase A using fluorescent adenosine derivatives Protein Sci. 9 2000 1818 1827
5. K. Tanaka, T. Kimura, and S. Maruta Synthesis of a novel fluorescent non-nucleotide ATP analogue and its interaction with myosin ATPase J. Biochem. 149 2011 395 403
6. D. Vertommen, L. Bertrand, B. Sontag, A. Di Pietro, M.P. Louckx, H. Vidal, L. Hue, and M.H. Rider The ATP-binding site in the 2-kinase domain of liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase J. Biol. Chem. 271 1996 17875 17880
7. F. Heitz, M.C. Morris, D. Fesquet, J.C. Cavadore, M. Dorée, and G. Divita Interactions of cyclins with cyclin-dependent kinases: a common interactive mechanism Biochemistry 36 1997 4995 5003 (Pubitemid 27180982)
8. M. Erdorf, and R. Seifert Pharmacological characterization of adenylyl cyclase isoforms in rabbit kidney membranes Naunyn Schmiedebergs Arch. Pharmacol. 383 2011 357 372
9. B.A. Witthuhn, F.W. Quelle, O. Silvennoinen, T. Yi, B. Tang, O. Miura, and J.N. Ihle JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin Cell 74 1993 227 236 (Pubitemid 23221699)
10. O. Silvennoinen, B.A. Witthuhn, F.W. Quelle, J.L. Cleveland, T. Yi, and J.N. Ihle Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction Proc. Natl. Acad. Sci. U.S.A 90 1993 8429 8433 (Pubitemid 23277682)
11. C. Haan, S. Kreis, C. Margue, and I. Behrmann Jaks and cytokine receptors - an intimate relationship Biochem. Pharmacol. 72 2006 1538 1546 (Pubitemid 44666728)
12. J. Boudeau, D. Miranda-Saavedra, G.J. Barton, and D.R. Alessi Emerging roles of pseudokinases Trends Cell Biol. 16 2006 443 452 (Pubitemid 44293399)
13. D. Ungureanu, J. Wu, T. Pekkala, Y. Niranjan, C. Young, O.N. Jensen, C.F. Xu, T.A. Neubert, R.C. Skoda, and S.R. Hubbard The pseudokinase domain of JAK2 is a dual-specificity protein kinase that negatively regulates cytokine signaling Nat. Struct. Mol. Biol. 18 2011 971 976
14. P. Saharinen, K. Takaluoma, and O. Silvennoinen Regulation of the Jak2 tyrosine kinase by its pseudokinase domain Sci. Signal. 20 2000 3387 3395 (Pubitemid 30243884)
15. A. Sanz, D. Ungureanu, T. Pekkala, R. Ruijtenbeek, I.P. Touw, R. Hilhorst, and O. Silvennoinen Analysis of Jak2 catalytic function by peptide microarrays: the role of the JH2 domain and V617F mutation PLoS One 6 2011 e18522
16. P. Saharinen, M. Vihinen, and O. Silvennoinen Autoinhibition of Jak2 tyrosine kinase is dependent on specific regions in its pseudokinase domain Mol. Biol. Cell 14 2003 1448 1459 (Pubitemid 36547413)
17. J.H. Kurzer, L.S. Argetsinger, Y.J. Zhou, J.L.K. Kouadio, J.J. O'Shea, and C. Carter-Su Tyrosine 813 is a site of JAK2 autophosphorylation critical for activation of JAK2 by SH2-Bβ Mol. Cell. Biol. 24 2004 4557 4570 (Pubitemid 44109138)
18. T. Hall, T.L. Emmons, J.E. Chrencik, J.A. Gormley, R.A. Weinberg, J.W. Leone, J.L. Hirsch, M.J. Saabye, J.F. Schindler, and J.E. Day Expression, purification, characterization, and crystallization of non- and phosphorylated states of JAK2 and JAK3 kinase domain Protein Expr. Purif. 69 2010 54 63
19. G. Divita, R. Goody, D. Gautheron, and A. Di Pietro Structural mapping of catalytic site with respect to α-subunit and noncatalytic site in yeast mitochondrial F1-ATPase using fluorescence resonance energy transfer J. Biol. Chem. 268 1993 13178 13186 (Pubitemid 23307735)
20. E. Zeqiraj, B.M. Filippi, S. Goldie, I. Navratilova, J. Boudeau, M. Deak, D.R. Alessi, and D.M.F. van Aalten ATP and MO25α regulate the conformational state of the STRADα pseudokinase and activation of the LKB1 tumour suppressor PLoS Biol. 7 2009 e1000126
21. K. Cheng, and J.G. Koland Nucleotide binding by the epidermal growth factor receptor protein-tyrosine kinase: Trinitrophenyl-ATP as a spectroscopic probe J. Biol. Chem. 271 1996 311 318
22. A.Y. Jan, E.F. Johnson, A.J. Diamonti, K.L. Carraway III, and K.S. Anderson Insights into the HER-2 receptor tyrosine kinase mechanism and substrate specificity using a transient kinetic analysis Biochemistry 39 2000 9786 9803 (Pubitemid 30627553)
23. F. Shi, S.E. Telesco, Y. Liu, R. Radhakrishnan, and M.A. Lemmon ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation Proc. Natl. Acad. Sci. U.S.A. 107 2010 7692 7697
24. M. Kubista, R. Sjöback, S. Eriksson, and B. Albinsson Experimental correction for the inner-filter effect in fluorescence spectra Analyst 119 1994 417 419
25. M. van de Weert Fluorescence quenching to study protein-ligand binding: common errors J. Fluoresc. 20 2010 625 629
26. M.L. Mertens, and J.H.R. Kägi A graphical correction procedure for inner filter effect in fluorescence quenching titrations Anal. Biochem. 96 1979 448 455 (Pubitemid 9230588)
27. B. Birdsall, R.W. King, M.R. Wheeler, C.A. Lewis Jr., S.R. Goode, R.B. Dunlap, and G.C.K. Roberts Correction for light absorption in fluorescence studies of protein-ligand interactions Anal. Biochem. 132 1983 353 361
28. N.K. Subbarao, and R.C. MacDonald Experimental method to correct fluorescence intensities for the inner filter effect Analyst 118 1993 913 916
29. Y. Liu, W. Kati, C.M. Chen, R. Tripathi, A. Molla, and W. Kohlbrenner Use of a fluorescence plate reader for measuring kinetic parameters with inner filter effect correction Anal. Biochem. 267 1999 331 335 (Pubitemid 29095880)
30. B. Van der Meer Kappa-squared: from nuisance to new sense Rev. Mol. Biotechnol. 82 2002 181 196 (Pubitemid 34179600)
31. 2+ Arch. Biochem. Biophys. 505 2011 60 66