Characterization of neuronal Src kinase purified from a bacterial expression system

Protein Expression and Purification

Volumn 74, Issue 2, 2010, Pages 289-297

  Marin, Vedrana ^a   Groveman, Bradley R ^a   Qiao, Haifa ^a   Xu, Jindong ^b   Ali, Mohammad K ^a   Fang, Xiao Qian ^a   Lin, Shuang Xiu ^a   Rizkallah, Raed ^a   Hurt, Myra H ^a   Bienkiewicz, Ewa A ^a   Yu, Xian Min ^a,b  

^a FLORIDA STATE UNIVERSITY COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

Denaturation; Kinase activity; Neuronal Src; Stability; Unfolding

Indexed keywords

ADENOSINE TRIPHOSPHATE; ISOENZYME; PROTEIN TYROSINE KINASE; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; ANIMAL; ARTICLE; CHEMISTRY; ESCHERICHIA COLI; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOUSE; POINT MUTATION; PROTEIN FOLDING;

ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; ANIMALS; ESCHERICHIA COLI; ISOENZYMES; MICE; POINT MUTATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SRC-FAMILY KINASES;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 77957753453     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.06.004     Document Type: Article

References (45)

1. R.C. Hsueh, and R.H. Scheuermann Tyrosine kinase activation in the decision between growth, differentiation, and death responses initiated from the B cell antigen receptor Adv. Immunol. 75 2000 283 316
2. X.-M. Yu, R. Askalan, G.J. Keil II, and M.W. Salter NMDA channel regulation by channel-associated protein tyrosine kinase Src Science 275 1997 674 678
3. L.V. Kalia, J.R. Gingrich, and M.W. Salter Src in synaptic transmission and plasticity Oncogene 23 2004 8007 8016
4. M.T. Brown, and J.A. Cooper Regulation, substrates and functions of src Biochim. Biophys. Acta 1287 1996 121 149
5. S.M. Thomas, and J.S. Brugge Cellular functions regulated by Src family kinases Annu. Rev. Cell Dev. Biol. 13 1997 513 609
6. c-src contains a six-amino acid insertion relative to its non-neuronal counterpart Science 237 1987 411 415
7. M. Inomata, Y. Takayama, H. Kiyama, S. Nada, M. Okada, and H. Nakagawa Regulation of Src family kinases in the developing rat brain: correlation with their regulator kinase, Csk J. Biochem. 116 1994 386 392
8. S. Nada, M. Okada, A. MacAuley, J.A. Cooper, and H. Nakagawa Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src Nature 351 1991 69 72
9. J. Xu, M. Weerapura, M.K. Ali, M.F. Jackson, H. Li, G. Lei, S. Xue, C.L. Kwan, M.F. Manolson, K. Yang, J.F. MacDonald, and X.M. Yu Control of excitatory synaptic transmission by C-terminal Src kinase J. Biol. Chem. 283 2008 17503 17514
10. S. Messina, F. Onofri, L. Bongiorno-Borbone, S. Giovedi, F. Valtorta, J.A. Girault, and F. Benfenati Specific interactions of neuronal focal adhesion kinase isoforms with Src kinases and amphiphysin J. Neurochem. 84 2003 253 265
11. J.M. Martin-Garcia, I. Luque, P.L. Mateo, J. Ruiz-Sanz, and A. Cámara-Artigas Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation FEBS Lett. 581 2007 1701 1706
12. T. Kotani, N. Morone, S. Yuasa, S. Nada, and M. Okada Constitutive activation of neuronal Src causes aberrant dendritic morphogenesis in mouse cerebellar Purkinje cells Neurosci. Res. 57 2007 210 219
13. W. Xu, S.C. Harrison, and M.J. Eck Three-dimensional structure of the tyrosine kinase c-Src Nature 385 1997 595 602
14. E. Ingley Src family kinases: regulation of their activities, levels and identification of new pathways Biochim. Biophys. Acta 1784 2008 56 65
15. Anthony Grabski, Mark Mehler, and Don Drott The overnight express autoinduction system: high-density cell growth and protein expression while you sleep Nat. Methods 2 2005 233 235
16. R.W. Woody Theory of circular dichroism in proteins G.D. Fasman, Circular Dichroism and the Conformational Analysis of Biomolecules 1996 Plenum Press New York 25 67
17. N. Sreerama, S.Y. Venyaminov, and R.W. Woody Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis Anal. Biochem. 287 2000 243 251
18. V. Rangachari, V. Marin, E.A. Bienkiewicz, M. Semavina, L. Guerrero, J.F. Love, J.R. Murphy, and T.M. Logan Sequence of ligand binding and structure change in the diphtheria toxin repressor upon activation by divalent transition metals Biochemistry 44 2005 5672 5682
19. N.S. de Groot, and S. Ventura Effect of temperature on protein quality in bacterial inclusion bodies FEBS Lett. 580 2006 6471 6476
20. S.M. Singh, and A.K. Panda Solubilization and refolding of bacterial inclusion body proteins J. Biosci. Bioeng. 99 2005 303 310
21. M. Susa, and A. Teti Tyrosine kinase src inhibitors: potential therapeutic applications Drug News Perspect. 13 2000 169 175
22. D.J. Kemble, Y.H. Wang, and G. Sun Bacterial expression and characterization of catalytic loop mutants of SRC protein tyrosine kinase Biochemistry 45 2006 14749 14754
23. T.R. Polte, and S.K. Hanks Complexes of focal adhesion kinase (FAK) and Crk-associated substrate (p130(Cas)) are elevated in cytoskeleton-associated fractions following adhesion and Src transformation. Requirements for Src kinase activity and FAK proline-rich motifs J. Biol. Chem. 272 1997 5501 5509
24. M. Osusky, S.J. Taylor, and D. Shalloway Autophosphorylation of purified c-Src at its primary negative regulation site J. Biol. Chem. 270 1995 25729 25732
25. 505 are autophosphorylated in recombinant Lck protein-tyrosine kinase expressed in Escherichia coli Eur. J. Biochem. 224 1994 589 596
26. C. Duy, and J. Fitter How aggregation and conformational scrambling of unfolded states govern fluorescence emission spectra Biophys. J. 90 2006 3704 3711
27. C. Duy, and J. Fitter Thermostability of irreversible unfolding alpha-amylases analyzed by unfolding kinetics J. Biol. Chem. 280 2005 37360 37365
28. R. Karni, S. Mizrachi, E. Reiss-Sklan, A. Gazit, O. Livnah, and A. Levitzki The pp60c-Src inhibitor PP1 is non-competitive against ATP FEBS Lett. 537 2003 47 52
29. J. Bain, H. McLauchlan, M. Elliott, and P. Cohen The specificities of protein kinase inhibitors: an update Biochem. J. 371 2003 199 204
30. P. Traxler, G. Bold, J. Frei, M. Lang, N. Lydon, H. Mett, E. Buchdunger, T. Meyer, M. Mueller, and P. Furet Use of a pharmacophore model for the design of EGF-R tyrosine kinase inhibitors: 4-(phenylamino)pyrazolo[3,4-d]pyrimidines J. Med. Chem. 40 1997 3601 3616 (Pubitemid 27465092)
31. B.J. Bennion, and V. Daggett The molecular basis for the chemical denaturation of proteins by urea Proc. Natl. Acad. Sci. USA 100 2003 5142 5147
32. C. Tanford Protein denaturation Adv. Protein Chem. 23 1968 121 282
33. H.J. Zhang, X.R. Sheng, X.M. Pan, and J.M. Zhou Activation of adenylate kinase by denaturants is due to the increasing conformational flexibility at its active sites Biochem. Biophys. Res. Commun. 238 1997 382 386
34. B.M. Baynes, D.I. Wang, and B.L. Trout Role of arginine in the stabilization of proteins against aggregation Biochemistry 44 2005 4919 4925
35. K. Tsumoto, M. Umetsu, I. Kumagai, D. Ejima, J.S. Philo, and T. Arakawa Role of arginine in protein refolding, solubilization, and purification Biotechnol. Prog. 20 2004 1301 1308
36. S.H. Lee, J.F. Carpenter, B.S. Chang, T.W. Randolph, and Y.S. Kim Effects of solutes on solubilization and refolding of proteins from inclusion bodies with high hydrostatic pressure Protein Sci. 15 2006 304 313
37. K.R.C. Reddy, H. Lilie, R. Rudolph, and C. Lange l-Arginine increases the solubility of unfolded species of hen egg white lysozyme Protein Sci. 14 2005 929 935
38. S.F. Falsone, S. Leptihn, A. Osterauer, M. Haslbeck, and J. Buchner Oncogenic mutations reduce the stability of SRC kinase J. Mol. Biol. 344 2004 281 291
39. S.C. Harrison Variation on an Src-like theme Cell 112 2003 737 740
40. F. Sicheri, and J. Kuriyan Structures of Src-family tyrosine kinases Curr. Opin. Struct. Biol. 7 1997 777 785
41. P. Filippakopoulos, M. Kofler, O. Hantschel, G.D. Gish, F. Grebien, E. Salah, P. Neudecker, L.E. Kay, B.E. Turk, G. Superti-Furga, T. Pawson, and S. Knapp Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation Cell 134 2008 793 803
42. T. Arakawa, D. Ejima, K. Tsumoto, N. Obeyama, Y. Tanaka, Y. Kita, and S.N. Timasheff Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects Biophys. Chem. 127 2007 1 8
43. A.S. Woods The mighty arginine, the stable quaternary amines, the powerful aromatics, and the aggressive phosphate: their role in the noncovalent minuet J. Proteome Res. 3 2004 478 484
44. Z. Weng, R.J. Rickles, S. Feng, S. Richard, A.S. Shaw, S.L. Schreiber, and J.S. Brugge Structure-function analysis of SH3 domains: SH3 binding specificity altered by single amino acid substitutions Mol. Cell. Biol. 15 1995 5627 5634
45. A. Zarrine-Afsar, A. Mittermaier, L.E. Kay, and A.R. Davidson Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain Protein Sci. 15 2006 162 170