메뉴 건너뛰기




Volumn 411, Issue 2, 2011, Pages 223-229

A practical method for cell-free protein synthesis to avoid stable isotope scrambling and dilution

Author keywords

Amino acid selective labeling; Cell free protein synthesis; Deuterium labeling; NMR; Stable isotope labeling

Indexed keywords

AMINO ACIDS; CELLS; CYTOLOGY; ESCHERICHIA COLI; ISOTOPES; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

EID: 79952452377     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2011.01.017     Document Type: Article
Times cited : (50)

References (53)
  • 1
    • 33846285730 scopus 로고    scopus 로고
    • Solution NMR of large molecules and assemblies
    • DOI 10.1021/bi0621314
    • M.P. Foster, C.A. McElroy, and C.D. Amero Solution NMR of large molecules and assemblies Biochemistry 46 2007 331 340 (Pubitemid 46115942)
    • (2007) Biochemistry , vol.46 , Issue.2 , pp. 331-340
    • Foster, M.P.1    McElroy, C.A.2    Amero, C.D.3
  • 2
    • 0000061511 scopus 로고
    • 15N enriched proteins: Application to triple resonance 4D J connectivity of sequential amides
    • 15N enriched proteins: application to triple resonance 4D J connectivity of sequential amides J. Am. Chem. Soc. 115 1993 4369 4370
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4369-4370
    • Grzesiek, S.1    Anglister, J.2    Ren, H.3    Bax, A.4
  • 4
    • 35448953299 scopus 로고    scopus 로고
    • Cell-free protein synthesis of perdeuterated proteins for NMR studies
    • DOI 10.1007/s10858-007-9188-0
    • T. Etezady-Esfarjani, S. Hiller, C. Villalba, and K. Wüthrich Cell-free protein synthesis of perdeuterated proteins for NMR studies J. Biomol. NMR 39 2007 229 238 (Pubitemid 47617507)
    • (2007) Journal of Biomolecular NMR , vol.39 , Issue.3 , pp. 229-238
    • Etezady-Esfarjani, T.1    Hiller, S.2    Villalba, C.3    Wuthrich, K.4
  • 6
    • 0242407224 scopus 로고    scopus 로고
    • Ile, Leu, and Val Methyl Assignments of the 723-Residue Malate Synthase G Using a New Labeling Strategy and Novel NMR Methods
    • DOI 10.1021/ja030345s
    • V. Tugarinov, and L.E. Kay Ile, Leu, and Val methyl assignments of the 723-residue malate synthase G using a new labeling strategy and novel NMR methods J. Am. Chem. Soc. 125 2003 13868 13878 (Pubitemid 37386061)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.45 , pp. 13868-13878
    • Tugarinov, V.1    Kay, L.E.2
  • 7
    • 33644774471 scopus 로고    scopus 로고
    • Optimal isotope labelling for NMR protein structure determinations
    • DOI 10.1038/nature04525, PII N04525
    • M. Kainosho, T. Torizawa, Y. Iwashita, T. Terauchi, A. Mei Ono, and P. Guntert Optimal isotope labelling for NMR protein structure determinations Nature 440 2006 52 57 (Pubitemid 43336263)
    • (2006) Nature , vol.440 , Issue.7080 , pp. 52-57
    • Kainosho, M.1    Torizawa, T.2    Iwashita, Y.3    Terauchi, T.4    Mei Ono, A.5    Guntert, P.6
  • 9
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • DOI 10.1016/S0014-5793(98)01620-2, PII S0014579398016202
    • T. Kigawa, T. Yabuki, Y. Yoshida, M. Tsutsui, Y. Ito, T. Shibata, and S. Yokoyama Cell-free production and stable-isotope labeling of milligram quantities of proteins FEBS Lett. 442 1999 15 19 (Pubitemid 29065369)
    • (1999) FEBS Letters , vol.442 , Issue.1 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3    Tsutsui, M.4    Ito, Y.5    Shibata, T.6    Yokoyama, S.7
  • 11
    • 0029365773 scopus 로고
    • Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis
    • T. Kigawa, Y. Muto, and S. Yokoyama Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis J. Biomol. NMR 6 1995 129 134
    • (1995) J. Biomol. NMR , vol.6 , pp. 129-134
    • Kigawa, T.1    Muto, Y.2    Yokoyama, S.3
  • 13
    • 14344256801 scopus 로고    scopus 로고
    • Cell-free protein production and labeling protocol for NMR-based structural proteomics
    • D. Vinarov, B. Lytle, F. Peterson, E. Tyler, B. Volkman, and J. Markley Cell-free protein production and labeling protocol for NMR-based structural proteomics Nat. Methods 1 2004 149 153
    • (2004) Nat. Methods , vol.1 , pp. 149-153
    • Vinarov, D.1    Lytle, B.2    Peterson, F.3    Tyler, E.4    Volkman, B.5    Markley, J.6
  • 16
    • 1242272915 scopus 로고    scopus 로고
    • Protein signal assignments using specific labeling and cell-free synthesis
    • DOI 10.1023/B:JNMR.0000013697.10256.74
    • J. Shi, J.G. Pelton, H.S. Cho, and D.E. Wemmer Protein signal assignments using specific labeling and cell-free synthesis J. Biomol. NMR 28 2004 235 247 (Pubitemid 38220172)
    • (2004) Journal of Biomolecular NMR , vol.28 , Issue.3 , pp. 235-247
    • Shi, J.1    Pelton, J.G.2    Cho, H.S.3    Wemmer, D.E.4
  • 19
    • 77952751010 scopus 로고    scopus 로고
    • Cell-free protein production system with the E. coli crude extract for determination of protein folds
    • T. Kigawa Cell-free protein production system with the E. coli crude extract for determination of protein folds Methods Mol. Biol. 607 2010 101 111
    • (2010) Methods Mol. Biol. , vol.607 , pp. 101-111
    • Kigawa, T.1
  • 20
    • 78651309787 scopus 로고    scopus 로고
    • An economical method for producing stable-isotope-labeled proteins by the E. coli cell-free system
    • J. Yokoyama, T. Matsuda, S. Koshiba, and T. Kigawa An economical method for producing stable-isotope-labeled proteins by the E. coli cell-free system J. Biomol. NMR 48 2010 193 201
    • (2010) J. Biomol. NMR , vol.48 , pp. 193-201
    • Yokoyama, J.1    Matsuda, T.2    Koshiba, S.3    Kigawa, T.4
  • 21
    • 55749110716 scopus 로고    scopus 로고
    • Production of membrane proteins using cell-free expression systems
    • D. Schwarz, V. Dötsch, and F. Bernhard Production of membrane proteins using cell-free expression systems Proteomics 8 2008 3933 3946
    • (2008) Proteomics , vol.8 , pp. 3933-3946
    • Schwarz, D.1    Dötsch, V.2    Bernhard, F.3
  • 22
    • 70349473228 scopus 로고    scopus 로고
    • Production of functional bacteriorhodopsin by an Escherichia coli cell-free protein synthesis system supplemented with steroid detergent and lipid
    • K. Shimono, M. Goto, T. Kikukawa, S. Miyauchi, M. Shirouzu, N. Kamo, and S. Yokoyama Production of functional bacteriorhodopsin by an Escherichia coli cell-free protein synthesis system supplemented with steroid detergent and lipid Protein Sci. 18 2009 2160 2171
    • (2009) Protein Sci. , vol.18 , pp. 2160-2171
    • Shimono, K.1    Goto, M.2    Kikukawa, T.3    Miyauchi, S.4    Shirouzu, M.5    Kamo, N.6    Yokoyama, S.7
  • 23
    • 76549098201 scopus 로고    scopus 로고
    • An Escherichia coli-based cell-free system for large-scale production of functional mammalian membrane proteins suitable for X-ray crystallography
    • T.A. Nguyen, S.S. Lieu, and G. Chang An Escherichia coli-based cell-free system for large-scale production of functional mammalian membrane proteins suitable for X-ray crystallography J. Mol. Microbiol. Biotechnol. 18 2010 85 91
    • (2010) J. Mol. Microbiol. Biotechnol. , vol.18 , pp. 85-91
    • Nguyen, T.A.1    Lieu, S.S.2    Chang, G.3
  • 24
    • 9644274089 scopus 로고    scopus 로고
    • The mechanism of α-proton isotope exchange in amino acids catalysed by tyrosine phenol-lyase: What is the role of quinonoid intermediates?
    • DOI 10.1111/j.1432-1033.2004.04428.x
    • N.G. Faleev, T.V. Demidkina, M.A. Tsvetikova, R.S. Phillips, and I.A. Yamskov The mechanism of α-proton isotope exchange in amino acids catalysed by tyrosine phenol-lyase: what is the role of quinonoid intermediates? Eur. J. Biochem. 271 2004 4565 4571 (Pubitemid 39576573)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.22 , pp. 4565-4571
    • Faleev, N.G.1    Demidkina, T.V.2    Tsvetikova, M.A.3    Phillips, R.S.4    Yamskov, I.A.5
  • 26
    • 0029929594 scopus 로고    scopus 로고
    • The effect of different amino acid side chains on the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the α-protons of amino acids
    • J.J. Milne, and J.P. Malthouse The effect of different amino acid side chains on the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the α-protons of amino acids Biochem. J. 314 1996 787 791 (Pubitemid 26097737)
    • (1996) Biochemical Journal , vol.314 , Issue.3 , pp. 787-791
    • Milne, J.J.1    Malthouse, J.P.G.2
  • 27
    • 0032519626 scopus 로고    scopus 로고
    • A substrate-induced change in the stereospecificity of the serine-hydroxymethyltransferase-catalysed exchange of the α-protons of amino acids. Evidence for a second catalytic site
    • DOI 10.1046/j.1432-1327.1998.2520113.x
    • T.B. Fitzpatrick, and J.P. Malthouse A substrate-induced change in the stereospecificity of the serine-hydroxymethyltransferase-catalysed exchange of the α-protons of amino acids: evidence for a second catalytic site Eur. J. Biochem. 252 1998 113 117 (Pubitemid 28089965)
    • (1998) European Journal of Biochemistry , vol.252 , Issue.1 , pp. 113-117
    • Fitzpatrick, T.B.1    Malthouse, J.P.G.2
  • 28
    • 0027331059 scopus 로고
    • The use of cystathionine γ-synthase in the production of α and chiral β deuterated amino acids
    • R.J. Homer, M.S. Kim, and D.M. LeMaster The use of cystathionine γ-synthase in the production of α and chiral β deuterated amino acids Anal. Biochem. 215 1993 211 215
    • (1993) Anal. Biochem. , vol.215 , pp. 211-215
    • Homer, R.J.1    Kim, M.S.2    Lemaster, D.M.3
  • 29
    • 0022271357 scopus 로고
    • H NMR studies of substrate hydrogen exchange reactions catalyzed by L-methionine γ-lyase
    • DOI 10.1021/bi00336a007
    • 1H NMR studies of substrate hydrogen exchange reactions catalyzed by l-methionine γ-lyase Biochemistry 24 1985 3857 3862 (Pubitemid 16239786)
    • (1985) Biochemistry , vol.24 , Issue.15 , pp. 3857-3862
    • Esaki, N.1    Nakayama, T.2    Sawada, S.3
  • 30
    • 0032712167 scopus 로고    scopus 로고
    • The aspartate aminotransferase-catalysed exchange of the α-protons of aspartate and glutamate: The effects of the R386A and R292V mutations on this exchange reaction
    • DOI 10.1016/S0167-4838(99)00181-8, PII S0167483899001818
    • M.M. Mahon, R. Graber, P. Christen, and J.P. Malthouse The aspartate aminotransferase-catalysed exchange of the α-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction Biochim. Biophys. Acta 1434 1999 191 201 (Pubitemid 29521346)
    • (1999) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1434 , Issue.1 , pp. 191-201
    • Mahon, M.M.1    Graber, R.2    Christen, P.3    Malthouse, J.P.G.4
  • 31
    • 0035909091 scopus 로고    scopus 로고
    • Characterization of inhibitors acting at the synthetase site of Escherichia coli asparagine synthetase B
    • DOI 10.1021/bi0155551
    • S.K. Boehlein, T. Nakatsu, J. Hiratake, R. Thirumoorthy, J.D. Stewart, N.G. Richards, and S.M. Schuster Characterization of inhibitors acting at the synthetase site of Escherichia coli asparagine synthetase B Biochemistry 40 2001 11168 11175 (Pubitemid 32847985)
    • (2001) Biochemistry , vol.40 , Issue.37 , pp. 11168-11175
    • Boehlein, S.K.1    Nakatsu, T.2    Hiratake, J.3    Thirumoorthy, R.4    Stewart, J.D.5    Richards, N.G.J.6    Schuster, S.M.7
  • 32
    • 0033597605 scopus 로고    scopus 로고
    • A potent transition-state analogue inhibitor of Escherichia coli asparagine synthetase A
    • DOI 10.1021/ja990851a
    • M. Koizumi, J. Hiratake, T. Nakatsu, H. Kato, and J.I. Oda A potent transition-state analogue inhibitor of Escherichia coli asparagine synthetase A J. Am. Chem. Soc. 121 1999 5799 5800 (Pubitemid 29300108)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.24 , pp. 5799-5800
    • Koizumi, M.1    Hiratake, J.2    Nakatsu, T.3    Kato, H.4    Oda, J.5
  • 34
    • 0014403696 scopus 로고
    • 5-Diazo-4-oxo-l-norvaline: Reactive asparagine analog with biological specificity
    • R.E. Handschumacher, C.J. Bates, P.K. Chang, A.T. Andrews, and G.A. Fischer 5-Diazo-4-oxo-l-norvaline: reactive asparagine analog with biological specificity Science 161 1968 62 63
    • (1968) Science , vol.161 , pp. 62-63
    • Handschumacher, R.E.1    Bates, C.J.2    Chang, P.K.3    Andrews, A.T.4    Fischer, G.A.5
  • 36
    • 0017891848 scopus 로고
    • The reaction of amino-oxyacetate with pyridoxal phosphate-dependent enzymes
    • R.A. John, A. Charteris, and L.J. Fowler The reaction of amino-oxyacetate with pyridoxal phosphate-dependent enzymes Biochem. J. 171 1978 771 779 (Pubitemid 8348755)
    • (1978) Biochemical Journal , vol.171 , Issue.3 , pp. 771-779
    • John, R.A.1    Charteris, A.2    Fowler, L.J.3
  • 37
    • 0014526454 scopus 로고
    • Identification of l-methionine S-sulfoximine as the diastereoisomer of l-methionine S,R-sulfoximine that inhibits glutamine synthetase
    • J.M. Manning, S. Moore, W.B. Rowe, and A. Meister Identification of l-methionine S-sulfoximine as the diastereoisomer of l-methionine S,R-sulfoximine that inhibits glutamine synthetase Biochemistry 8 1969 2681 2685
    • (1969) Biochemistry , vol.8 , pp. 2681-2685
    • Manning, J.M.1    Moore, S.2    Rowe, W.B.3    Meister, A.4
  • 38
    • 0024298585 scopus 로고
    • L-Aspartase from Escherichia coli: Substrate specificity and role of divalent metal ions
    • C.J. Falzone, W.E. Karsten, J.D. Conley, and R.E. Viola l-Aspartase from Escherichia coli: substrate specificity and role of divalent metal ions Biochemistry 27 1988 9089 9093
    • (1988) Biochemistry , vol.27 , pp. 9089-9093
    • Falzone, C.J.1    Karsten, W.E.2    Conley, J.D.3    Viola, R.E.4
  • 39
    • 0014408695 scopus 로고
    • Glutaminase of Escherichia coli: 3. Studies on the reaction mechanism
    • S.C. Hartman Glutaminase of Escherichia coli: 3. Studies on the reaction mechanism J. Biol. Chem. 243 1968 870 878
    • (1968) J. Biol. Chem. , vol.243 , pp. 870-878
    • Hartman, S.C.1
  • 41
    • 0016366135 scopus 로고
    • Asparagine utilization in Escherichia coli
    • R.C. Willis, and C.A. Woolfolk Asparagine utilization in Escherichia coli J. Bacteriol. 118 1974 231 241
    • (1974) J. Bacteriol. , vol.118 , pp. 231-241
    • Willis, R.C.1    Woolfolk, C.A.2
  • 42
    • 44349161779 scopus 로고    scopus 로고
    • Residues Asp164 and Glu165 at the substrate entryway function potently in substrate orientation of alanine racemase from E. coli: Enzymatic characterization with crystal structure analysis
    • DOI 10.1110/ps.083495908
    • D. Wu, T. Hu, L. Zhang, J. Chen, J. Du, J. Ding, H. Jiang, and X. Shen Residues Asp164 and Glu165 at the substrate entryway function potently in substrate orientation of alanine racemase from E. coli: enzymatic characterization with crystal structure analysis Protein Sci. 17 2008 1066 1076 (Pubitemid 351749212)
    • (2008) Protein Science , vol.17 , Issue.6 , pp. 1066-1076
    • Wu, D.1    Hu, T.2    Zhang, L.3    Chen, J.4    Du, J.5    Ding, J.6    Jiang, H.7    Shen, X.8
  • 43
    • 0020642713 scopus 로고
    • 6 activity of L-penicillamine in Escherichia coli
    • R. Yamada Antivitamin B6 activity of l-penicillamine in Escherichia coli Acta Vitaminol. Enzymol. 5 1983 73 81 (Pubitemid 13027571)
    • (1983) Acta Vitaminologica et Enzymologica , vol.5 , Issue.2 , pp. 73-81
    • Yamada, R.1
  • 46
    • 0025900995 scopus 로고
    • A novel α-proton exchange reaction catalyzed by Escherichia coli methionyl-tRNA synthetase
    • J. Williams, and P. Rosevear A novel α-proton exchange reaction catalyzed by Escherichia coli methionyl-tRNA synthetase Biochemistry 30 1991 6412 6416
    • (1991) Biochemistry , vol.30 , pp. 6412-6416
    • Williams, J.1    Rosevear, P.2
  • 47
    • 0025972759 scopus 로고
    • Cysteinyl-tRNA synthetase: Determination of the last E.coli aminoacyl-tRNA synthetase primary structure
    • G. Eriani, G. Dirheimer, and J. Gangloff Cysteinyl-tRNA synthetase: determination of the last E. coli aminoacyl-tRNA synthetase primary structure Nucleic Acids Res. 19 1991 265 269 (Pubitemid 21896968)
    • (1991) Nucleic Acids Research , vol.19 , Issue.2 , pp. 265-269
    • Eriani, G.1    Dirheimer, G.2    Gangloff, J.3
  • 48
    • 0025371584 scopus 로고
    • Proofreading in vivo: Editing of homocysteine by methionyl-tRNA synthetase in Escherichia coli
    • H. Jakubowski Proofreading in vivo: editing of homocysteine by methionyl-tRNA synthetase in Escherichia coli Proc. Natl. Acad. Sci. USA 87 1990 4504 4508
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4504-4508
    • Jakubowski, H.1
  • 49
    • 0028217884 scopus 로고
    • Editing function of Escherichia coli cysteinyl-tRNA synthetase: Cyclization of cysteine to cysteine thiolactone
    • H. Jakubowski Editing function of Escherichia coli cysteinyl-tRNA synthetase: cyclization of cysteine to cysteine thiolactone Nucleic Acids Res. 22 1994 1155 1160 (Pubitemid 24162117)
    • (1994) Nucleic Acids Research , vol.22 , Issue.7 , pp. 1155-1160
    • Jakubowski, H.1
  • 52
    • 3242686114 scopus 로고    scopus 로고
    • Amino acid stabilization for cell-free protein synthesis by modification of the Escherichia coli genome
    • DOI 10.1016/j.ymben.2004.01.003, PII S1096717604000151
    • N. Michel-Reydellet, K. Calhoun, and J. Swartz Amino acid stabilization for cell-free protein synthesis by modification of the Escherichia coli genome Metab. Eng. 6 2004 197 203 (Pubitemid 38946637)
    • (2004) Metabolic Engineering , vol.6 , Issue.3 , pp. 197-203
    • Michel-Reydellet, N.1    Calhoun, K.2    Swartz, J.3
  • 53
    • 43049126791 scopus 로고    scopus 로고
    • Cell-free protein synthesis system from Escherichia coli cells cultured at decreased temperatures improves productivity by decreasing DNA template degradation
    • E. Seki, N. Matsuda, S. Yokoyama, and T. Kigawa Cell-free protein synthesis system from Escherichia coli cells cultured at decreased temperatures improves productivity by decreasing DNA template degradation Anal. Biochem. 377 2008 156 161
    • (2008) Anal. Biochem. , vol.377 , pp. 156-161
    • Seki, E.1    Matsuda, N.2    Yokoyama, S.3    Kigawa, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.