15N-labelled proteins by cell-free protein synthesis: Strategies for high-throughput NMR studies of proteins and protein-ligand complexes

FEBS Journal

Volumn 273, Issue 18, 2006, Pages 4154-4159

  Ozawa, Kiyoshi ^a   Wu, Peter S C ^a   Dixon, Nicholas E ^a   Otting, Gottfried ^a  

^a AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

Author keywords

15N HSQC; 15N labelled amino acids; Cell free protein synthesis; Combinatorial labelling; Protein ligand interactions

Indexed keywords

AMINO ACID; AMINOTRANSFERASE; ASPARAGINE; ASPARTIC ACID; CELL EXTRACT; ISOTOPE; NITROGEN 15; PROLINE; LIGAND; NITROGEN; PROTEIN;

AMINO ACID ANALYSIS; AMINO ACID METABOLISM; CELL FREE SYSTEM; CELL GROWTH; CHROMATOGRAPHY; ENZYME ACTIVITY; ENZYME REPRESSION; ESCHERICHIA COLI; HIGH THROUGHPUT SCREENING; ISOTOPE LABELING; MACROMOLECULE; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; QUANTUM MECHANICS; SHORT SURVEY; CHEMISTRY; METABOLISM; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE; REVIEW;

CELL-FREE SYSTEM; LIGANDS; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BIOSYNTHESIS; PROTEINS;

EID: 33748311913     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05433.x     Document Type: Short Survey

References (27)

1. Kigawa T, Muto Y & Yokoyama S (1995) Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis. J Biomol NMR 6, 129-134.
2. Kigawa T, Yabuki T, Yoshida Y, Tsutsui M, Ito Y, Shibata T & Yokoyama S (1999) Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett 442, 15-19.
3. Madin K, Sawasaki T, Ogasawara T & Endo Y (2000) A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: Plants apparently contain a suicide system directed at ribosomes. Proc Natl Acad Sci USA 97, 559-564.
4. Yokoyama S (2003) Protein expression systems for structural genomics and proteomics. Curr Opin Chem Biol 7, 39-43.
5. Vinarov DA, Lytle BL, Peterson FC, Tyler EM, Volkman BF & Markley JL (2004) Cell-free protein production and labeling protocol for NMR-based structural proteomics. Nat Methods 1, 149-153.
6. Kainosho M, Torizawa T, Iwashita Y, Terauchi T, Ono AM & Güntert P (2006) Optimal isotope labelling for NMR protein structure determinations. Nature 440, 52-57.
7. 15N-labeled proteins for NMR studies. IUBMB Life 57, 615-622.
8. Kigawa T, Yamaguchi-Nunokawa E, Kodama K, Matsuda T, Yabuki T, Matsuda N, Ishitani R, Nureki O & Yokoyama S (2001) Selenomethionine incorporation into a protein by cell-free synthesis. J Struct Funct Genomics 2, 29-35.
9. Ozawa K, Headlam MJ, Mouradov D, Watt SJ, Beck JL, Rodgers KJ, Dean RT, Huber T, Otting G & Dixon NE (2005) Translational incorporation of L-3,4-dihydroxyphenylalanine into proteins. FEBS J 272, 3162-3171.
10. 15N-labelling. J Biomol NMR 34, 13-21.
11. Ozawa K, Jergic S, Crowther JA, Thompson PR, Wijffels G, Otting G & Dixon NE (2005) Cell-free in vitro protein synthesis in an autoinduction system for NMR studies of protein-protein interactions. J Biomol NMR 32, 235-241.
12. Kainosho M & Tsuji T (1982) Assignment of the three methionyl carbon resonances in Streptomyces subtilisin inhibitor by a carbon-13 and nitrogen-15 double labeling technique. A new strategy for structural studies of proteins in solution. Biochemistry 21, 6273-6279.
13. 15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type. Biochemistry 24, 7263-7268.
14. Griffey RH, Redfield AG, Loomis RE & Dahlquist FW (1985) Nuclear magnetic resonance observation and dynamics of specific amide protons in T4 lysozyme. Biochemistry 24, 817-822.
15. 13C for assignment and interpretation of nuclear magnetic resonance spectra of proteins. Q Rev Biophys 23, 1-38.
16. 15N resonances and secondary structure of ribonuclease H from Escherichia coli by heteronuclear three-dimensional NMR spectroscopy. Biochemistry 30, 6036-6047.
17. 14N-amino acids. J Magn Reson B 105, 88-90.
18. 15N-labelled proteins for rapid analysis by NMR spectroscopy. Eur J Biochem 271, 4084-4093.
19. Klammt C, Löhr F, Schäfer B, Haase W, Dötsch V, Rüterjans H, Glaubitz C & Bernhard F (2004) High-level cell-free expression and specific labeling of integral membrane proteins. Eur J Biochem 271, 568-580.
20. 15N HSQC spectra with a wheat germ cell-free protein synthesis system. J Biomol NMR 30, 37-45.
21. Guignard L, Ozawa K, Pursglove SE, Otting G & Dixon NE (2002) NMR analysis of in vitro-synthesized proteins without purification: a high-throughput approach. FEBS Lett 524, 159-162.
22. Keppetipola S, Kudlicki W, Nguyen BD, Meng X, Donovan KJ & Shaka AJ (2006) From gene to HSQC in under five hours: high-throughput NMR proteomics. J Am Chem Soc 128, 4508-4509.
23. Shi J, Pelton JG, Cho HS & Wemmer DE (2004) Protein signal assignments using specific labeling and cell-free synthesis. J Biomol NMR 28, 235-247.
24. Trbovic N, Klammt C, Koglin A, Löhr F & Bernhard & Dötsch V (2005) Efficient strategy for the rapid backbone assignment of membrane proteins. J Am Chem Soc 127, 13504-13505.
25. Parker MJ, Aulton-Jones M, Hounslow AM & Craven CJ (2004) A combinatorial selective labeling method for the assignment of backbone amide NMR resonances. J Am Chem Soc 126, 5020-5021.
26. Yabuki T, Kigawa T, Dohmae N, Takio K, Terada T, Ito Y, Laue ED, Cooper JA, Kainosho M & Yokoyama S (1998) Dual amino acid-selective and site-directed stable-isotope labeling of the human c-Ha-Ras protein by cell-free synthesis. J Biomol NMR 11, 295-306.
27. Emerson SD, Palermo R, Liu CM, Tilley JW, Chen L, Danho W, Madison VS, Greeley DN, Ju G & Fry DC (2003) NMR characterization of interleukin-2 in complexes with the IL-2Rα receptor component, and with low molecular weight compounds that inhibit the IL-2/IL-Rα interaction. Protein Sci 12, 811-822.