NMR spectroscopy as a tool for the rapid assessment of the conformation of GST-fusion proteins

Protein Science

Volumn 17, Issue 9, 2008, Pages 1630-1635

  Chu, Kong Liew ^a   Gamsjaeger, Roland ^a   Mansfield, Robyn E ^a   Mackay, Joel P ^a  

^a UNIVERSITY OF SYDNEY   (Australia)

Author keywords

GST fusion; GST pulldown; NMR spectroscopy; Protein conformation

Indexed keywords

GLUTATHIONE TRANSFERASE; HYBRID PROTEIN;

ARTICLE; CHEMICAL ANALYSIS; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SCREENING;

ANIMALS; BUFFERS; CAENORHABDITIS ELEGANS PROTEINS; DIMERIZATION; EVALUATION STUDIES AS TOPIC; GLUTATHIONE TRANSFERASE; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; TIME FACTORS;

EID: 50049088243     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.034983.108     Document Type: Article

References (26)

1. Braun, P., Hu, Y., Shen, B., Halleck, A., Koundinya, M., Harlow, E., and LaBaer, J. 2002. Proteome-scale purification of human proteins from bacteria. Proc. Natl. Acad. Sci. 99: 2654-2659.
2. Brymora, A., Valova, V.A., and Robinson, P.J 2004. Protein-protein interactions identified by pulldown experiments and mass spectrometry. In Current protocols in cell biology, Section 17.5. Unlimited Learning Resources, Winston-Salem, NC.
3. Catanzariti, A.M., Soboleva, T.A., Jans, D.A., Board, P.G., and Baker, R.T. 2004. An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci. 13: 1331-1339.
4. Christodoulou, J., Larsson, G., Fucini, P., Connell, S.R., Pertinhez, T.A., Hanson, C.L., Redfield, C., Nierhaus, K.H., Robinson, C.V., Schleucher, J., et al. 2004. Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes. Proc. Natl. Acad. Sci. 101: 10949-10954.
5. Folta-Stogniew, E. and Williams, K. 1999. Determination of molecular masses of proteins in solution: Implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory. J. Biomol. Tech. 10: 51-63.
6. Fox, A.H., Kowalski, K., King, G.F., Mackay, J.P., and Crossley, M. 1998. Key residues characteristic of GATA N-fingers are recognized by FOG. J. Biol. Chem. 273: 33595-33603.
7. Gamsjaeger, R., Swanton, M.K., Kobus, F.J., Lehtomaki, E., Lowry, J.A., Kwan, A.H., Matthews, J.M., and Mackay, J.P. 2007. Structural and biophysical analysis of the DNA-binding properties of myelin transcription factor 1. J. Biol. Chem. 283: 5158-5167.
8. Hammarstrom, M., Hellgren, N., van Den Berg, S., Berglund, H., and Hard, T. 2002. Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci. 11: 313-321.
9. Huth, J.R., Bewley, C.A., Jackson, B.M., Hinnebusch, A.G., Clore, G.M., and Gronenborn, A.M. 1997. Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR. Protein Sci. 6: 2359-2364.
10. Jeon, W.B., Aceti, D.J., Bingman, C.A., Vojtik, F.C., Olson, A.C., Ellefson, J.M., McCombs, J.E., Sreenath, H.K., Blommel, P.G., Seder, K.D., et al. 2005. High-throughput purification and quality assurance of Arabidopsis thaliana proteins for eukaryotic structural genomics. J. Struct. Funct. Genomics 6: 143-147.
11. LaVallie, E.R., Lu, Z., Diblasio-Smith, E.A., Collins-Racie, L.A., and McCoy, J.M. 2000. Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli. Methods Enzymol. 326: 322-340.
12. Lee, B.M., Buck-Koehntop, B.A., Martinez-Yamout, M.A., Dyson, H.J., and Wright, P.E. 2007. Embryonic neural inducing factor Churchill is not a DNA-binding zinc finger protein: Solution structure reveals a solvent-exposed β-sheet and zinc binuclear cluster. J. Mol. Biol. 371: 1274-1289.
13. Liew, C.K., Crossley, M., Mackay, J.P., and Nicholas, H.R. 2007. Solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP). J. Mol. Biol. 366: 382-390.
14. Masino, L., Kelly, G., Leonard, K., Trottier, Y., and Pastore, A. 2002. Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins. FEBS Lett. 513: 267-272.
15. Masters, S.L., Yao, S., Willson, T.A., Zhang, J.G., Palmer, K.R., Smith, B.J., Babon, J.J., Nicola, N.A., Norton, R.S., and Nicholson, S.E. 2006. The SPRY domain of SSB-2 adopts a novel fold that presents conserved Par-4-binding residues. Nat. Struct. Mol. Biol. 13: 77-84.
16. Mulder, F.A., Bouakaz, L., Lundell, A., Venkataramana, M., Liljas, A., Akke, M., and Sanyal, S. 2004. Conformation and dynamics of ribosomal stalk protein L12 in solution and on the ribosome. Biochemistry 43: 5930-5936.
17. Riley, L.G., Ralston, G.B., and Weiss, A.S. 1996. Multimer formation as a consequence of separate homodimerization domains: The human c-Jun leucine zipper is a transplantable dimerization module. Protein Eng. 9: 223-230.
18. 15N relaxation measurements. Biochemistry 33: 13997-14002.
19. Sachdev, D. and Chirgwin, J.M. 2000. Fusions to maltose-binding protein: Control of folding and solubility in protein purification. Methods Enzymol. 326: 312-321.
20. Sakashita, E. and Sakamoto, H. 1994. Characterization of RNA binding specificity of the Drosophila sex-lethal protein by in vitro ligand selection. Nucleic Acids Res. 22: 4082-4086.
21. Smith, D.B. 2000. Generating fusions to glutathione S-transferase for protein studies. Methods Enzymol. 326: 254-270.
22. 15N NMR relaxation measurements. Biochemistry 32: 426-435.
23. Tang, C., Ndassa, Y., and Summers, M.F. 2002. Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. Nat. Struct. Biol. 9: 537-543.
24. Tugarinov, V., Muhandiram, R., Ayed, A., and Kay, L.E. 2002. Four-dimensional NMR spectroscopy of a 723-residue protein: Chemical shift assignments and secondary structure of malate synthase G. J. Am. Chem. Soc. 124: 10025-10035.
25. Tyler, R.C., Aceti, D.J., Bingman, C.A., Cornilescu, C.C., Fox, B.G., Frederick, R.O., Jeon, W.B., Lee, M.S., Newman, C.S., Peterson, F.C., et al. 2005. Comparison of cell-based and cell-free protocols for producing target proteins from the Arabidopsis thaliana genome for structural studies. Proteins 59: 633-643.
26. 15N NMR relaxation. Biochemistry 34: 5212-5223.