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Volumn 57, Issue 3, 2013, Pages 297-304

Perdeuteration and methyl-selective 1H, 13C-labeling by using a Kluyveromyces lactis expression system

Author keywords

Eukaryotic expression system; Kluyveromyces lactis; Large molecular weight protein; Methyl selective 1H, 13C labeling; Perdeuteration; Stable isotope labeling

Indexed keywords

BACTERIAL PROTEIN; BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE; CARBON 13; METHYL GROUP; PROTON;

EID: 84890119562     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-013-9789-8     Document Type: Article
Times cited : (24)

References (18)
  • 1
    • 79251536260 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Bat1 and Bat2 aminotransferases have functionally diverged from the ancestral-like Kluyveromyces lactis orthologous enzyme
    • 2011PLoSO.616099C 10.1371/journal.pone.0016099
    • Colón M, Hernández F, López K, Quezada H, González J, López G, Aranda C, González A (2011) Saccharomyces cerevisiae Bat1 and Bat2 aminotransferases have functionally diverged from the ancestral-like Kluyveromyces lactis orthologous enzyme. PLoS One 6:e16099
    • (2011) PLoS One , vol.6 , pp. 16099
    • Colón, M.1    Hernández, F.2    López, K.3    Quezada, H.4    González, J.5    López, G.6    Aranda, C.7    González, A.8
  • 2
    • 0032544978 scopus 로고    scopus 로고
    • Solution NMR studies of a 42 KDa Escherichia Coli maltose binding protein/β-cyclodextrin complex: Chemical shift assignments and analysis
    • 10.1021/ja982019w
    • Gardner KH, Zhang X, Gehring K, Kay LE (1998) Solution NMR studies of a 42 KDa Escherichia Coli maltose binding protein/β-cyclodextrin complex: chemical shift assignments and analysis. J Am Chem Soc 120:11738-11748
    • (1998) J Am Chem Soc , vol.120 , pp. 11738-11748
    • Gardner, K.H.1    Zhang, X.2    Gehring, K.3    Kay, L.E.4
  • 3
    • 84855276227 scopus 로고    scopus 로고
    • A simple protocol for amino acid type selective isotope labeling in insect cells with improved yields and high reproducibility
    • 10.1007/s10858-011-9570-9
    • Gossert AD, Hinniger A, Gutmann S, Jahnke W, Strauss A, Fernández C (2011) A simple protocol for amino acid type selective isotope labeling in insect cells with improved yields and high reproducibility. J Biomol NMR 51:449-456
    • (2011) J Biomol NMR , vol.51 , pp. 449-456
    • Gossert, A.D.1    Hinniger, A.2    Gutmann, S.3    Jahnke, W.4    Strauss, A.5    Fernández, C.6
  • 4
    • 0037354160 scopus 로고    scopus 로고
    • A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes
    • 10.1023/A:1022890112109
    • Gross JD, Gelev VM, Wagner G (2003) A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes. J Biomol NMR 25:235-242
    • (2003) J Biomol NMR , vol.25 , pp. 235-242
    • Gross, J.D.1    Gelev, V.M.2    Wagner, G.3
  • 5
    • 3042661951 scopus 로고    scopus 로고
    • Rapid isolation of yeast genomic DNA: Bust n' Grab
    • 10.1186/1472-6750-4-8
    • Harju S, Fedosyuk H, Peterson K (2004) Rapid isolation of yeast genomic DNA: bust n' Grab. BMC Biotechnol 4:8
    • (2004) BMC Biotechnol , vol.4 , pp. 8
    • Harju, S.1    Fedosyuk, H.2    Peterson, K.3
  • 6
    • 1942452749 scopus 로고    scopus 로고
    • Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae
    • 2004Natur.428.617K 10.1038/nature02424
    • Kellis M, Birren BW, Lander ES (2004) Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae. Nature 428:617-624
    • (2004) Nature , vol.428 , pp. 617-624
    • Kellis, M.1    Birren, B.W.2    Lander, E.S.3
  • 7
    • 77955323388 scopus 로고    scopus 로고
    • Theoretical analyses of the transferred cross-saturation method
    • 2010JMagR.205.114M 10.1016/j.jmr.2010.04.011
    • Matsumoto M, Ueda T, Shimada I (2010) Theoretical analyses of the transferred cross-saturation method. J Magn Reson 205:114-124
    • (2010) J Magn Reson , vol.205 , pp. 114-124
    • Matsumoto, M.1    Ueda, T.2    Shimada, I.3
  • 8
    • 0033816837 scopus 로고    scopus 로고
    • Expression of deuterium-isotope-labelled protein in the yeast Pichia pastoris for NMR studies
    • 10.1023/A:1008313530207
    • Morgan WD, Kragt A, Feeney J (2000) Expression of deuterium-isotope- labelled protein in the yeast Pichia pastoris for NMR studies. J Biomol NMR 17:337-347
    • (2000) J Biomol NMR , vol.17 , pp. 337-347
    • Morgan, W.D.1    Kragt, A.2    Feeney, J.3
  • 9
    • 0016124816 scopus 로고
    • Subcellular localization of isoleucine-valine biosynthetic enzymes in yeast
    • Ryan ED, Kohlhaw GB (1974) Subcellular localization of isoleucine-valine biosynthetic enzymes in yeast. J Bacteriol 120:631-637
    • (1974) J Bacteriol , vol.120 , pp. 631-637
    • Ryan, E.D.1    Kohlhaw, G.B.2
  • 10
    • 0015911466 scopus 로고
    • Subcellular localization of the leucine biosynthetic enzymes in yeast
    • Ryan ED, Tracy JW, Kohlhaw GB (1973) Subcellular localization of the leucine biosynthetic enzymes in yeast. J Bacteriol 116:222-225
    • (1973) J Bacteriol , vol.116 , pp. 222-225
    • Ryan, E.D.1    Tracy, J.W.2    Kohlhaw, G.B.3
  • 11
    • 80051663513 scopus 로고    scopus 로고
    • Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy
    • 10.1007/s10858-011-9506-4
    • Sastry M, Xu L, Georgiev IS, Bewley CA, Nabel GJ, Kwong PD (2011) Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy. J Biomol NMR 50:197-207
    • (2011) J Biomol NMR , vol.50 , pp. 197-207
    • Sastry, M.1    Xu, L.2    Georgiev, I.S.3    Bewley, C.A.4    Nabel, G.J.5    Kwong, P.D.6
  • 13
    • 3042652967 scopus 로고    scopus 로고
    • Amino acid biosynthesis and metabolic flux profiling of Pichia pastoris
    • 10.1111/j.1432-1033.2004.04176.x
    • Solà A, Maaheimo H, Ylönen K, Ferrer P, Szyperski T (2004) Amino acid biosynthesis and metabolic flux profiling of Pichia pastoris. Eur J Biochem 271:2462-2470
    • (2004) Eur J Biochem , vol.271 , pp. 2462-2470
    • Solà, A.1    Maaheimo, H.2    Ylönen, K.3    Ferrer, P.4    Szyperski, T.5
  • 14
    • 33846268057 scopus 로고    scopus 로고
    • Metabolic flux profiling of Pichia pastoris grown on glycerol/methanol mixtures in chemostat cultures at low and high dilution rates
    • 10.1099/mic.0.29263-0
    • Solà A, Jouhten P, Maaheimo H, Sánchez-Ferrando F, Szyperski T, Ferrer P (2007) Metabolic flux profiling of Pichia pastoris grown on glycerol/methanol mixtures in chemostat cultures at low and high dilution rates. Microbiology 153:281-290
    • (2007) Microbiology , vol.153 , pp. 281-290
    • Solà, A.1    Jouhten, P.2    Maaheimo, H.3    Sánchez-Ferrando, F.4    Szyperski, T.5    Ferrer, P.6
  • 15
    • 55649087551 scopus 로고    scopus 로고
    • Stable isotope labeling of protein by Kluyveromyces lactis for NMR study
    • 10.1007/s10858-008-9276-9
    • Sugiki T, Shimada I, Takahashi H (2008) Stable isotope labeling of protein by Kluyveromyces lactis for NMR study. J Biomol NMR 42:159-162
    • (2008) J Biomol NMR , vol.42 , pp. 159-162
    • Sugiki, T.1    Shimada, I.2    Takahashi, H.3
  • 16
    • 0034051065 scopus 로고    scopus 로고
    • A novel NMR method for determining the interfaces of large protein-protein complexes
    • 10.1038/73331
    • Takahashi H, Nakanishi T, Kami K, Arata Y, Shimada I (2000) A novel NMR method for determining the interfaces of large protein-protein complexes. Nat Struct Biol 7:220-223
    • (2000) Nat Struct Biol , vol.7 , pp. 220-223
    • Takahashi, H.1    Nakanishi, T.2    Kami, K.3    Arata, Y.4    Shimada, I.5
  • 17
    • 0041930989 scopus 로고    scopus 로고
    • 13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes
    • 10.1021/ja030153x
    • 13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. J Am Chem Soc 125:10420-10428
    • (2003) J Am Chem Soc , vol.125 , pp. 10420-10428
    • Tugarinov, V.1    Hwang, P.M.2    Ollerenshaw, J.E.3    Kay, L.E.4
  • 18
    • 33846998346 scopus 로고    scopus 로고
    • Probing side-chain dynamics in the proteasome by relaxation violated coherence transfer NMR spectroscopy
    • 10.1021/ja067827z
    • Tugarinov V, Sprangers R, Kay LE (2007) Probing side-chain dynamics in the proteasome by relaxation violated coherence transfer NMR spectroscopy. J Am Chem Soc 129:1743-1750
    • (2007) J Am Chem Soc , vol.129 , pp. 1743-1750
    • Tugarinov, V.1    Sprangers, R.2    Kay, L.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.