메뉴 건너뛰기




Volumn 7, Issue 7, 2012, Pages

Fluorescent in situ folding control for rapid optimization of cell-free membrane protein synthesis

Author keywords

[No Author keywords available]

Indexed keywords

AQUAGLYCEROPORIN; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; PROTEOLIPOSOME;

EID: 84864415088     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0042186     Document Type: Article
Times cited : (23)

References (32)
  • 3
    • 33645454462 scopus 로고    scopus 로고
    • Optimization of membrane protein overexpression and purification using GFP fusions
    • Drew D, Lerch M, Kunji E, Slotboom DJ, de Gier JW,((2006)) Optimization of membrane protein overexpression and purification using GFP fusions. Nat Methods 3:: 303--313.
    • (2006) Nat Methods , vol.3 , pp. 303-313
    • Drew, D.1    Lerch, M.2    Kunji, E.3    Slotboom, D.J.4    de Gier, J.W.5
  • 4
    • 35348832935 scopus 로고    scopus 로고
    • High-throughput fluorescent-based optimization of eukaryotic membrane protein overexpression and purification in Saccharomyces cerevisiae
    • Newstead S, Kim H, von Heijne G, Iwata S, Drew D,((2007)) High-throughput fluorescent-based optimization of eukaryotic membrane protein overexpression and purification in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 104:: 13936--13941.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 13936-13941
    • Newstead, S.1    Kim, H.2    von Heijne, G.3    Iwata, S.4    Drew, D.5
  • 5
    • 80053141646 scopus 로고    scopus 로고
    • GFP-based evaluation system of recombinant expression through the secretory pathway in insect cells and its application to the extracellular domains of class C GPCRs
    • Ashikawa Y, Ihara M, Matsuura N, Fukunaga Y, Kusakabe Y, et al.((2011)) GFP-based evaluation system of recombinant expression through the secretory pathway in insect cells and its application to the extracellular domains of class C GPCRs. Protein Sci 20:: 1720--1734.
    • (2011) Protein Sci , vol.20 , pp. 1720-1734
    • Ashikawa, Y.1    Ihara, M.2    Matsuura, N.3    Fukunaga, Y.4    Kusakabe, Y.5
  • 6
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin AS, Baranov VI, Ryabova LA, Ovodov SY, Alakhov YB,((1988)) A continuous cell-free translation system capable of producing polypeptides in high yield. Science 242:: 1162--1164.
    • (1988) Science , vol.242 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 7
    • 39149143698 scopus 로고    scopus 로고
    • Preparative scale expression of membrane proteins in Escherichia coli-based continuous exchange cell-free systems
    • Schwarz D, Junge F, Durst F, Frölich N, Schneider B, et al.((2007)) Preparative scale expression of membrane proteins in Escherichia coli-based continuous exchange cell-free systems. Nat Protocols 2:: 2945--2957.
    • (2007) Nat Protocols , vol.2 , pp. 2945-2957
    • Schwarz, D.1    Junge, F.2    Durst, F.3    Frölich, N.4    Schneider, B.5
  • 8
    • 28244458078 scopus 로고    scopus 로고
    • Evaluation of detergents for the soluble expression of α-helical and β-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system
    • Klammt C, Schwarz D, Fendler K, Haase W, Dötsch V, et al.((2005)) Evaluation of detergents for the soluble expression of α-helical and β-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system. FEBS J 272:: 6024--6038.
    • (2005) FEBS J , vol.272 , pp. 6024-6038
    • Klammt, C.1    Schwarz, D.2    Fendler, K.3    Haase, W.4    Dötsch, V.5
  • 9
    • 69249095799 scopus 로고    scopus 로고
    • Cell-free synthesis of functional aquaporin Z in synthetic liposomes
    • Hovijitra NT, Wuu JJ, Peaker B, Swartz JR,((2009)) Cell-free synthesis of functional aquaporin Z in synthetic liposomes. Biotechnol Bioeng 104:: 40--49.
    • (2009) Biotechnol Bioeng , vol.104 , pp. 40-49
    • Hovijitra, N.T.1    Wuu, J.J.2    Peaker, B.3    Swartz, J.R.4
  • 10
    • 84934436148 scopus 로고    scopus 로고
    • Cell-free expression for nanolipoprotein particles: building a high-throughput membrane protein solubility platform
    • Cappuccio JA, Hinz AK, Kuhn EA, Fletcher JE, Arroyo ES, et al.((2009)) Cell-free expression for nanolipoprotein particles: building a high-throughput membrane protein solubility platform. Methods Mol Biol 498:: 273--296.
    • (2009) Methods Mol Biol , vol.498 , pp. 273-296
    • Cappuccio, J.A.1    Hinz, A.K.2    Kuhn, E.A.3    Fletcher, J.E.4    Arroyo, E.S.5
  • 11
    • 0037085374 scopus 로고    scopus 로고
    • A single, bi-functional aquaglyceroporin in blood-stage Plasmodium falciparum malaria parasites
    • Hansen M, Kun JF, Schultz JE, Beitz E,((2002)) A single, bi-functional aquaglyceroporin in blood-stage Plasmodium falciparum malaria parasites. J Biol Chem 277:: 4874--4882.
    • (2002) J Biol Chem , vol.277 , pp. 4874-4882
    • Hansen, M.1    Kun, J.F.2    Schultz, J.E.3    Beitz, E.4
  • 12
    • 0842342619 scopus 로고    scopus 로고
    • Molecular dissection of water and glycerol permeability of the aquaglyceroporin from Plasmodium falciparum by mutational analysis
    • Beitz E, Pavlovic-Djuranovic S, Yasui M, Agre P, Schultz JE,((2004)) Molecular dissection of water and glycerol permeability of the aquaglyceroporin from Plasmodium falciparum by mutational analysis. Proc Natl Acad Sci U S A 101:: 1153--1158.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 1153-1158
    • Beitz, E.1    Pavlovic-Djuranovic, S.2    Yasui, M.3    Agre, P.4    Schultz, J.E.5
  • 13
  • 15
    • 81855190805 scopus 로고    scopus 로고
    • The tetrameric α-helical membrane protein GlpF unfolds via a dimeric folding intermediate
    • Veerappan A, Cymer F, Klein N, Schneider D,((2011)) The tetrameric α-helical membrane protein GlpF unfolds via a dimeric folding intermediate. Biochemistry 50:: 10223--10230.
    • (2011) Biochemistry , vol.50 , pp. 10223-10230
    • Veerappan, A.1    Cymer, F.2    Klein, N.3    Schneider, D.4
  • 16
    • 0038131090 scopus 로고    scopus 로고
    • Chain length dependence of apomyoglobin folding: structural evolution from misfolded sheets to native helices
    • Chow CC, Chow C, Raghunathan V, Huppert TJ, Kimball EB, et al.((2003)) Chain length dependence of apomyoglobin folding: structural evolution from misfolded sheets to native helices. Biochemistry 42:: 7090--7099.
    • (2003) Biochemistry , vol.42 , pp. 7090-7099
    • Chow, C.C.1    Chow, C.2    Raghunathan, V.3    Huppert, T.J.4    Kimball, E.B.5
  • 17
    • 80052426196 scopus 로고    scopus 로고
    • Glycosylation increases the thermostability of human aquaporin 10 protein
    • Öberg F, Sjöhamn J, Fischer G, Moberg A, Pedersen A, et al.((2011)) Glycosylation increases the thermostability of human aquaporin 10 protein. J Biol Chem 286:: 31915--31923.
    • (2011) J Biol Chem , vol.286 , pp. 31915-31923
    • Öberg, F.1    Sjöhamn, J.2    Fischer, G.3    Moberg, A.4    Pedersen, A.5
  • 18
    • 33644499478 scopus 로고    scopus 로고
    • Monitoring protein aggregation during thermal unfolding in circular dichroism experiments
    • Benjwal S, Verma S, Röhm KH, Gursky O,((2006)) Monitoring protein aggregation during thermal unfolding in circular dichroism experiments. Protein Sci 15:: 635--639.
    • (2006) Protein Sci , vol.15 , pp. 635-639
    • Benjwal, S.1    Verma, S.2    Röhm, K.H.3    Gursky, O.4
  • 19
    • 84857763121 scopus 로고    scopus 로고
    • Molar concentrations of sorbitol and polyethylene glycol inhibit the Plasmodium aquaglyceroporin but not that of E. coli: involvement of the channel vestibules
    • Song J, Almasalmeh A, Krenc D, Beitz E,((2012)) Molar concentrations of sorbitol and polyethylene glycol inhibit the Plasmodium aquaglyceroporin but not that of E. coli: involvement of the channel vestibules. Biochim Biophys Acta 1818:: 1218--1224.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1218-1224
    • Song, J.1    Almasalmeh, A.2    Krenc, D.3    Beitz, E.4
  • 20
    • 0035861859 scopus 로고    scopus 로고
    • Characterisation of a concentrative type of adenosine transporter from Arabidopsis thaliana (ENT1,At)
    • Möhlmann T, Mezher Z, Schwerdtfeger G, Neuhaus HE,((2001)) Characterisation of a concentrative type of adenosine transporter from Arabidopsis thaliana (ENT1,At). FEBS Lett 509:: 370--374.
    • (2001) FEBS Lett , vol.509 , pp. 370-374
    • Möhlmann, T.1    Mezher, Z.2    Schwerdtfeger, G.3    Neuhaus, H.E.4
  • 21
    • 33847128735 scopus 로고    scopus 로고
    • The fluorouridine insensitive 1 (fur1) mutant is defective in equilibrative nucleoside transporter 3 (ENT3), and thus represents an important pyrimidine nucleoside uptake system in Arabidopsis thaliana
    • Traub M, Flörchinger M, Piecuch J, Kunz HH, Weise-Steinmetz A, et al.((2007)) The fluorouridine insensitive 1 (fur1) mutant is defective in equilibrative nucleoside transporter 3 (ENT3), and thus represents an important pyrimidine nucleoside uptake system in Arabidopsis thaliana. Plant J 49:: 855--864.
    • (2007) Plant J , vol.49 , pp. 855-864
    • Traub, M.1    Flörchinger, M.2    Piecuch, J.3    Kunz, H.H.4    Weise-Steinmetz, A.5
  • 22
    • 80052887466 scopus 로고    scopus 로고
    • Equilibrative nucleoside transporter 1 (ENT1) is critical for pollen germination and vegetative growth in Arabidopsis
    • Bernard C, Traub M, Kunz HH, Hach S, Trentmann O, et al.((2011)) Equilibrative nucleoside transporter 1 (ENT1) is critical for pollen germination and vegetative growth in Arabidopsis. J Exp Bot 62:: 4627--4637.
    • (2011) J Exp Bot , vol.62 , pp. 4627-4637
    • Bernard, C.1    Traub, M.2    Kunz, H.H.3    Hach, S.4    Trentmann, O.5
  • 24
    • 0029086174 scopus 로고
    • Cloning and regulation of expression of the rat kidney urea transporter (rUT2)
    • Smith CP, Lee WS, Martial S, Knepper MA, You G, et al.((1995)) Cloning and regulation of expression of the rat kidney urea transporter (rUT2). J Clin Invest 96:: 1556--1563.
    • (1995) J Clin Invest , vol.96 , pp. 1556-1563
    • Smith, C.P.1    Lee, W.S.2    Martial, S.3    Knepper, M.A.4    You, G.5
  • 25
    • 72049114961 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of the kidney urea transporter
    • Levin EJ, Quick M, Zhou M,((2009)) Crystal structure of a bacterial homologue of the kidney urea transporter. Nature 462:: 757--762.
    • (2009) Nature , vol.462 , pp. 757-762
    • Levin, E.J.1    Quick, M.2    Zhou, M.3
  • 26
    • 70849106457 scopus 로고    scopus 로고
    • Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel
    • Wang Y, Huang Y, Wang J, Cheng C, Huang W, et al.((2009)) Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel. Nature 462:: 467--473.
    • (2009) Nature , vol.462 , pp. 467-473
    • Wang, Y.1    Huang, Y.2    Wang, J.3    Cheng, C.4    Huang, W.5
  • 27
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien R,((1998)) The green fluorescent protein. Annu Rev Biochem 67:: 509--544.
    • (1998) Annu Rev Biochem , vol.67 , pp. 509-544
    • Tsien, R.1
  • 28
    • 79953802067 scopus 로고    scopus 로고
    • Production and partial purification of membrane proteins using a liposome-supplemented wheat cell-free translation system
    • Nozawa A, Ogasawara T, Matsunaga S, Iwasaki T, Sawasaki T, et al.((2011)) Production and partial purification of membrane proteins using a liposome-supplemented wheat cell-free translation system. BMC Biotechnol 11:: 35.
    • (2011) BMC Biotechnol , vol.11 , pp. 35
    • Nozawa, A.1    Ogasawara, T.2    Matsunaga, S.3    Iwasaki, T.4    Sawasaki, T.5
  • 29
    • 0032614376 scopus 로고    scopus 로고
    • GFP variants for multispectral imaging of living cells
    • Hasseloff J,((1999)) GFP variants for multispectral imaging of living cells. Methods Cell Biol 58:: 139--151.
    • (1999) Methods Cell Biol , vol.58 , pp. 139-151
    • Hasseloff, J.1
  • 30
    • 77958544345 scopus 로고    scopus 로고
    • Preparative scale production of functional mouse aquaporin 4 using different cell-free expression modes
    • Kai L, Kaldenhoff R, Lian J, Zhu X, Dötsch V, et al.((2010)) Preparative scale production of functional mouse aquaporin 4 using different cell-free expression modes. PLoS One 5:: e12972.
    • (2010) PLoS One , vol.5
    • Kai, L.1    Kaldenhoff, R.2    Lian, J.3    Zhu, X.4    Dötsch, V.5
  • 31
    • 58149156187 scopus 로고    scopus 로고
    • Structure-function analysis of plant aquaporin AtPIP2;1 gating by divalent cations and protons
    • Verdoucq L, Grondin A, Maurel C,((2006)) Structure-function analysis of plant aquaporin AtPIP2;1 gating by divalent cations and protons. Biochem J 415:: 409--416.
    • (2006) Biochem J , vol.415 , pp. 409-416
    • Verdoucq, L.1    Grondin, A.2    Maurel, C.3
  • 32
    • 33847134005 scopus 로고    scopus 로고
    • Aquaporin-11 containing a divergent NPA motif has normal water channel activity
    • Yakata K, Hiroaki Y, Ishibashi K, Sohara E, Sasaki S, et al.((2007)) Aquaporin-11 containing a divergent NPA motif has normal water channel activity. Biochim Biophys Acta 1768:: 688--693.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 688-693
    • Yakata, K.1    Hiroaki, Y.2    Ishibashi, K.3    Sohara, E.4    Sasaki, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.