메뉴 건너뛰기




Volumn 5, Issue 1, 2010, Pages

Lactococcus lactis, an alternative system for functional expression of peripheral and intrinsic arabidopsis membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; COMPLEMENTARY DNA; MEMBRANE PROTEIN;

EID: 77649279415     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0008746     Document Type: Article
Times cited : (37)

References (77)
  • 2
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E, von Heijne G (1998) Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci 7: 1029-1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 3
    • 13644265954 scopus 로고    scopus 로고
    • Protein secretion in Lactococcus lactis: An efficient way to increase the overall heterologous protein production
    • Le Loir Y, Azevedo V, Oliveira SC, Freitas DA, Miyoshi A, et al. (2005) Protein secretion in Lactococcus lactis: an efficient way to increase the overall heterologous protein production. Microb Cell Fact 4: 2.
    • (2005) Microb Cell Fact , vol.4 , pp. 2
    • Le Loir, Y.1    Azevedo, V.2    Oliveira, S.C.3    Freitas, D.A.4    Miyoshi, A.5
  • 4
    • 26844475027 scopus 로고    scopus 로고
    • Industrial-scale production and purification of a heterologous protein in Lactococcus lactis using the nisin-controlled gene expression system NICE: The case of lysostaphin
    • Mierau I, Leij P, van Swam I, Blommestein B, Floris E, et al. (2005) Industrial-scale production and purification of a heterologous protein in Lactococcus lactis using the nisin-controlled gene expression system NICE: the case of lysostaphin. Microb Cell Fact 4: 15.
    • (2005) Microb Cell Fact , vol.4 , pp. 15
    • Mierau, I.1    Leij, P.2    van Swam, I.3    Blommestein, B.4    Floris, E.5
  • 5
    • 26844435071 scopus 로고    scopus 로고
    • Optimization of the Lactococcus lactis nisin-controlled gene expression system NICE for industrial applications
    • Mierau I, Olieman K, Mond J, Smid EJ (2005) Optimization of the Lactococcus lactis nisin-controlled gene expression system NICE for industrial applications. Microb Cell Fact 4: 16.
    • (2005) Microb Cell Fact , vol.4 , pp. 16
    • Mierau, I.1    Olieman, K.2    Mond, J.3    Smid, E.J.4
  • 6
    • 33645872407 scopus 로고    scopus 로고
    • The nisin-controlled gene expression system: Construction, application and improvements
    • Zhou XX, Li WF, Ma GX, Pan YJ (2006) The nisin-controlled gene expression system: construction, application and improvements. Biotechnol Adv 24: 285-295.
    • (2006) Biotechnol Adv , vol.24 , pp. 285-295
    • Zhou, X.X.1    Li, W.F.2    Ma, G.X.3    Pan, Y.J.4
  • 7
    • 42349105761 scopus 로고    scopus 로고
    • Mucosal delivery of therapeutic and prophylactic molecules using lactic acid bacteria
    • Wells JM, Mercenier A (2008) Mucosal delivery of therapeutic and prophylactic molecules using lactic acid bacteria. Nat Rev Microbiol 6: 349-362.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 349-362
    • Wells, J.M.1    Mercenier, A.2
  • 8
    • 12444290982 scopus 로고    scopus 로고
    • Heterologous expression of the plant coumarate: CoA ligase in Lactococcus lactis
    • Martinez-Cuesta MC, Gasson MJ, Narbad A (2005) Heterologous expression of the plant coumarate: CoA ligase in Lactococcus lactis. Lett Appl Microbiol 40: 44-49.
    • (2005) Lett Appl Microbiol , vol.40 , pp. 44-49
    • Martinez-Cuesta, M.C.1    Gasson, M.J.2    Narbad, A.3
  • 11
    • 34247854960 scopus 로고    scopus 로고
    • Complete genome sequence of the prototype lactic acid bacterium Lactococcus lactis subsp. cremoris MG1363
    • Wegmann U, O'Connell-Motherway M, Zomer A, Buist G, Shearman C, et al. (2007) Complete genome sequence of the prototype lactic acid bacterium Lactococcus lactis subsp. cremoris MG1363. J Bacteriol 189: 3256-3270.
    • (2007) J Bacteriol , vol.189 , pp. 3256-3270
    • Wegmann, U.1    O'Connell-Motherway, M.2    Zomer, A.3    Buist, G.4    Shearman, C.5
  • 13
    • 27544451339 scopus 로고    scopus 로고
    • 10 years of the nisin-controlled gene expression system (NICE) in Lactococcus lactis
    • Mierau I, Kleerebezem M (2005) 10 years of the nisin-controlled gene expression system (NICE) in Lactococcus lactis. Appl Microbiol Biotechnol 68: 705-717.
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 705-717
    • Mierau, I.1    Kleerebezem, M.2
  • 14
    • 0037450575 scopus 로고    scopus 로고
    • Lactococcus lactis as host for overproduction of functional membrane proteins
    • Kunji ER, Slotboom DJ, Poolman B (2003) Lactococcus lactis as host for overproduction of functional membrane proteins. Biochim Biophys Acta 1610: 97-108.
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 97-108
    • Kunji, E.R.1    Slotboom, D.J.2    Poolman, B.3
  • 16
    • 0037033102 scopus 로고    scopus 로고
    • Non-canonical transit peptide for import into the chloroplast
    • Miras S, Salvi D, Ferro M, Grunwald D, Garin J, et al. (2002) Non-canonical transit peptide for import into the chloroplast. J Biol Chem 277: 47770-47778.
    • (2002) J Biol Chem , vol.277 , pp. 47770-47778
    • Miras, S.1    Salvi, D.2    Ferro, M.3    Grunwald, D.4    Garin, J.5
  • 17
    • 35748972640 scopus 로고    scopus 로고
    • TOC159- and TOC75-independent import of a transit sequence-less precursor into the inner envelope of chloroplasts
    • Miras S, Salvi D, Piette L, Seigneurin-Berny D, Grunwald D, et al. (2007) TOC159- and TOC75-independent import of a transit sequence-less precursor into the inner envelope of chloroplasts. J Biol Chem 282: 29482-29492.
    • (2007) J Biol Chem , vol.282 , pp. 29482-29492
    • Miras, S.1    Salvi, D.2    Piette, L.3    Seigneurin-Berny, D.4    Grunwald, D.5
  • 18
    • 25844489990 scopus 로고    scopus 로고
    • P(1B)-ATPases - an ancient family of transition metal pumps with diverse functions in plants
    • Williams LE, Mills RF (2005) P(1B)-ATPases - an ancient family of transition metal pumps with diverse functions in plants. Trends Plant Sci 10: 491-502.
    • (2005) Trends Plant Sci , vol.10 , pp. 491-502
    • Williams, L.E.1    Mills, R.F.2
  • 19
    • 33646128945 scopus 로고    scopus 로고
    • Put the metal to the petal: Metal uptake and transport throughout plants
    • Colangelo EP, Guerinot ML (2006) Put the metal to the petal: metal uptake and transport throughout plants. Curr Opin Plant Biol 9: 322-330.
    • (2006) Curr Opin Plant Biol , vol.9 , pp. 322-330
    • Colangelo, E.P.1    Guerinot, M.L.2
  • 20
    • 34248633103 scopus 로고    scopus 로고
    • The structure and function of heavy metal transport P1B-ATPases
    • Argüello JM, Eren E, González-Guerrero M (2007) The structure and function of heavy metal transport P1B-ATPases. Biometals 20: 233-248.
    • (2007) Biometals , vol.20 , pp. 233-248
    • Argüello, J.M.1    Eren, E.2    González-Guerrero, M.3
  • 21
    • 0037781037 scopus 로고    scopus 로고
    • PAA1, a P-type ATPase of Arabidopsis, functions in copper transport in chloroplasts
    • Shikanai T, Müller-Moulé P, Munekage Y, Niyogi KK, Pilon M (2003) PAA1, a P-type ATPase of Arabidopsis, functions in copper transport in chloroplasts. Plant Cell 15: 1333-1346.
    • (2003) Plant Cell , vol.15 , pp. 1333-1346
    • Shikanai, T.1    Müller-Moulé, P.2    Munekage, Y.3    Niyogi, K.K.4    Pilon, M.5
  • 22
    • 33646153414 scopus 로고    scopus 로고
    • HMA1, a new Cu-ATPase of the chloroplast envelope, is essential for growth under adverse light conditions
    • Seigneurin-Berny D, Gravot A, Auroy P, Mazard C, Kraut A, et al. (2006) HMA1, a new Cu-ATPase of the chloroplast envelope, is essential for growth under adverse light conditions. J Biol Chem 281: 2882-2892.
    • (2006) J Biol Chem , vol.281 , pp. 2882-2892
    • Seigneurin-Berny, D.1    Gravot, A.2    Auroy, P.3    Mazard, C.4    Kraut, A.5
  • 23
    • 60249091588 scopus 로고    scopus 로고
    • AtHMA3, a P1B-ATPase allowing Cd/Zn/Co/Pb vacuolar storage in Arabidopsis
    • Morel M, Crouzet J, Gravot A, Auroy P, Leonhardt N, et al. (2009) AtHMA3, a P1B-ATPase allowing Cd/Zn/Co/Pb vacuolar storage in Arabidopsis. Plant Physiol 149: 894-904.
    • (2009) Plant Physiol , vol.149 , pp. 894-904
    • Morel, M.1    Crouzet, J.2    Gravot, A.3    Auroy, P.4    Leonhardt, N.5
  • 24
    • 14244263503 scopus 로고    scopus 로고
    • Heavy metal transport by AtHMA4 involves the N-terminal degenerated metal binding domain and the C-terminal His11 stretch
    • Verret F, Gravot A, Auroy P, Preveral S, Forestier C, et al. (2005) Heavy metal transport by AtHMA4 involves the N-terminal degenerated metal binding domain and the C-terminal His11 stretch. FEBS Lett 579: 1515-1522.
    • (2005) FEBS Lett , vol.579 , pp. 1515-1522
    • Verret, F.1    Gravot, A.2    Auroy, P.3    Preveral, S.4    Forestier, C.5
  • 25
    • 12744254290 scopus 로고    scopus 로고
    • The plant P1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in detoxification of transition metals supplied at elevated levels
    • Mills RF, Francini A, Ferreira da Rocha PS, Baccarini PJ, Aylett M, et al. (2005) The plant P1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in detoxification of transition metals supplied at elevated levels. FEBS Lett 579: 783-791.
    • (2005) FEBS Lett , vol.579 , pp. 783-791
    • Mills, R.F.1    Francini, A.2    Ferreira da Rocha, P.S.3    Baccarini, P.J.4    Aylett, M.5
  • 26
    • 0031036197 scopus 로고    scopus 로고
    • Characterization of a novel eukaryotic ATP/ADP translocator located in the plastid envelope of Arabidopsis thaliana L
    • Neuhaus HE, Thom E, Möhlmann T, Steup M, Kampfenkel K (1997) Characterization of a novel eukaryotic ATP/ADP translocator located in the plastid envelope of Arabidopsis thaliana L. Plant J 11: 73-82.
    • (1997) Plant J , vol.11 , pp. 73-82
    • Neuhaus, H.E.1    Thom, E.2    Möhlmann, T.3    Steup, M.4    Kampfenkel, K.5
  • 27
    • 61349103765 scopus 로고    scopus 로고
    • Nonmitochondrial ATP/ADP transporters accept phosphate as third substrate
    • Trentmann O, Jung B, Neuhaus HE, Haferkamp I (2008) Nonmitochondrial ATP/ADP transporters accept phosphate as third substrate. J Biol Chem 283: 36486-36493.
    • (2008) J Biol Chem , vol.283 , pp. 36486-36493
    • Trentmann, O.1    Jung, B.2    Neuhaus, H.E.3    Haferkamp, I.4
  • 28
    • 0028822675 scopus 로고
    • Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate translocator of higher plants
    • Kampfenkel K, Möhlmann T, Batz O, Van Montagu M, Inzé D, et al. (1995) Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate translocator of higher plants. FEBS Lett 374: 351-355.
    • (1995) FEBS Lett , vol.374 , pp. 351-355
    • Kampfenkel, K.1    Möhlmann, T.2    Batz, O.3    Van Montagu, M.4    Inzé, D.5
  • 29
    • 0032439289 scopus 로고    scopus 로고
    • Altered plastidic ATP/ADP-transporter activity influences potato (Solanum tuberosum L.) tuber morphology, yield and composition of tuber starch
    • Tjaden J, Möhlmann T, Kampfenkel K, Henrichs G, Neuhaus HE (1998) Altered plastidic ATP/ADP-transporter activity influences potato (Solanum tuberosum L.) tuber morphology, yield and composition of tuber starch. Plant J 16: 531-540.
    • (1998) Plant J , vol.16 , pp. 531-540
    • Tjaden, J.1    Möhlmann, T.2    Kampfenkel, K.3    Henrichs, G.4    Neuhaus, H.E.5
  • 30
    • 34547102994 scopus 로고    scopus 로고
    • Expression vectors for the rapid purification of recombinant proteins in Bacillus subtilis
    • Nguyen HD, Phuong Phan TT, Schumann W (2007) Expression vectors for the rapid purification of recombinant proteins in Bacillus subtilis. Curr Microbiol 55: 89-93.
    • (2007) Curr Microbiol , vol.55 , pp. 89-93
    • Nguyen, H.D.1    Phuong Phan, T.T.2    Schumann, W.3
  • 31
    • 33845917294 scopus 로고    scopus 로고
    • A novel regulatory metal binding domain is present in the C terminus of Arabidopsis Zn2+-ATPase HMA2
    • Eren E, Kennedy DC, Maroney MJ, Argüello JM (2006) A novel regulatory metal binding domain is present in the C terminus of Arabidopsis Zn2+-ATPase HMA2. J Biol Chem 281: 33881-33891.
    • (2006) J Biol Chem , vol.281 , pp. 33881-33891
    • Eren, E.1    Kennedy, D.C.2    Maroney, M.J.3    Argüello, J.M.4
  • 33
    • 34548072799 scopus 로고    scopus 로고
    • Topology-informed strategies for the overexpression of membrane proteins
    • Rahman M, Ismat F, McPherson MJJ, Baldwin SA (2007) Topology-informed strategies for the overexpression of membrane proteins. Mol Memb Biol 24: 407-418.
    • (2007) Mol Memb Biol , vol.24 , pp. 407-418
    • Rahman, M.1    Ismat, F.2    McPherson, M.J.J.3    Baldwin, S.A.4
  • 34
    • 34250766201 scopus 로고    scopus 로고
    • The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins
    • Schmidt TG, Skerra A (2007) The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat Protoc 2: 1528-1535.
    • (2007) Nat Protoc , vol.2 , pp. 1528-1535
    • Schmidt, T.G.1    Skerra, A.2
  • 35
    • 0242300620 scopus 로고    scopus 로고
    • Empirical Analysis of Transcriptional Activity in the Arabidopsis Genome
    • Yamada K, Lim J, Dale JM, Chen H, Shinn P, et al. (2003) Empirical Analysis of Transcriptional Activity in the Arabidopsis Genome. Science 302: 842-846.
    • (2003) Science , vol.302 , pp. 842-846
    • Yamada, K.1    Lim, J.2    Dale, J.M.3    Chen, H.4    Shinn, P.5
  • 36
    • 4043153341 scopus 로고    scopus 로고
    • Versatile gene-specific sequence tags for Arabidopsis functional genomics: Transcript profiling and reverse genetics applications
    • Hilson P, Allemeersch J, Altmann T, Aubourg S, Avon A, et al. (2004) Versatile gene-specific sequence tags for Arabidopsis functional genomics: transcript profiling and reverse genetics applications. Genome Res 14: 2176-2189.
    • (2004) Genome Res , vol.14 , pp. 2176-2189
    • Hilson, P.1    Allemeersch, J.2    Altmann, T.3    Aubourg, S.4    Avon, A.5
  • 37
    • 0021217886 scopus 로고
    • Construction of plasmid cloning vectors for lactic streptococci which also replicate in Bacillus subtilis and Escherichia coli
    • Kok J, van der Vossen JM, Venema G (1984) Construction of plasmid cloning vectors for lactic streptococci which also replicate in Bacillus subtilis and Escherichia coli. Appl Environ Microbiol 48: 726-731.
    • (1984) Appl Environ Microbiol , vol.48 , pp. 726-731
    • Kok, J.1    van der Vossen, J.M.2    Venema, G.3
  • 38
    • 0002978298 scopus 로고
    • Gene cloning and expression systems in Lactococci
    • chapter 2, Gasson MJ, de Vos WM, eds, London: Blackie Academic and Professional. pp
    • de Vos WM, Simons GFM (1994) Gene cloning and expression systems in Lactococci, chapter 2. In: Gasson MJ, de Vos WM, eds. Genetics and Biotechnology of Lactic Acid Bacteria. London: Blackie Academic and Professional. pp 52-105.
    • (1994) Genetics and Biotechnology of Lactic Acid Bacteria , pp. 52-105
    • de Vos, W.M.1    Simons, G.F.M.2
  • 39
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer R, Tate CG (1995) Overexpression of integral membrane proteins for structural studies. Q Rev Biophys 28: 315-422.
    • (1995) Q Rev Biophys , vol.28 , pp. 315-422
    • Grisshammer, R.1    Tate, C.G.2
  • 40
    • 0037324955 scopus 로고    scopus 로고
    • Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs)
    • Persson B, Kallberg Y, Oppermann U, Jornvall H (2003) Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs). Chem Biol Interact 143/144: 271-278.
    • (2003) Chem Biol Interact , vol.143-144 , pp. 271-278
    • Persson, B.1    Kallberg, Y.2    Oppermann, U.3    Jornvall, H.4
  • 41
    • 0027202031 scopus 로고
    • Monoclonal antibodies for structure-function studies of (R)-3-hydroxybutyrate dehydrogenase, a lipid-dependent membrane-bound enzyme
    • Adami P, Duncan TM, McIntyre JO, Carter CE, Fu C, et al. (1993) Monoclonal antibodies for structure-function studies of (R)-3-hydroxybutyrate dehydrogenase, a lipid-dependent membrane-bound enzyme. Biochem J 292: 863-872.
    • (1993) Biochem J , vol.292 , pp. 863-872
    • Adami, P.1    Duncan, T.M.2    McIntyre, J.O.3    Carter, C.E.4    Fu, C.5
  • 42
    • 0037450544 scopus 로고    scopus 로고
    • Specific lipid requirements of membrane proteins - a putative bottleneck in heterologous expression
    • Opekarova M, Tanner W (2003) Specific lipid requirements of membrane proteins - a putative bottleneck in heterologous expression. Biochim Biophys Acta 1610: 11-22.
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 11-22
    • Opekarova, M.1    Tanner, W.2
  • 43
    • 33750477995 scopus 로고    scopus 로고
    • Calcium regulation of chloroplast protein translocation is mediated by calmodulin binding to Tic32
    • Chigri F, Hörmann F, Stamp A, Stammers DK, Bölter B, et al. (2006) Calcium regulation of chloroplast protein translocation is mediated by calmodulin binding to Tic32. Proc Natl Acad Sci U S A 103: 16051-16056.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 16051-16056
    • Chigri, F.1    Hörmann, F.2    Stamp, A.3    Stammers, D.K.4    Bölter, B.5
  • 44
    • 2642673614 scopus 로고    scopus 로고
    • Expression of a plastidic ATP/ADP transporter gene in Escherichia coli leads to a functional adenine nucleotide transport system in the bacterial cytoplasmic membrane
    • Tjaden J, Schwöppe C, Möhlmann T, Quick PW, Neuhaus HE (1998) Expression of a plastidic ATP/ADP transporter gene in Escherichia coli leads to a functional adenine nucleotide transport system in the bacterial cytoplasmic membrane. J Biol Chem 273: 9630-9636.
    • (1998) J Biol Chem , vol.273 , pp. 9630-9636
    • Tjaden, J.1    Schwöppe, C.2    Möhlmann, T.3    Quick, P.W.4    Neuhaus, H.E.5
  • 45
    • 0034234633 scopus 로고    scopus 로고
    • Increasing expression of P450 and P450-reductase proteins from monocots in heterologous systems
    • Batard Y, Hehn A, Nedelkina S, Schalk M, Pallett K, et al. (2000) Increasing expression of P450 and P450-reductase proteins from monocots in heterologous systems. Arch Biochem Biophys 379: 161-169.
    • (2000) Arch Biochem Biophys , vol.379 , pp. 161-169
    • Batard, Y.1    Hehn, A.2    Nedelkina, S.3    Schalk, M.4    Pallett, K.5
  • 47
    • 34548319070 scopus 로고    scopus 로고
    • High-throughput cloning and expression in recalcitrant bacteria
    • Geertsma ER, Poolman B (2007) High-throughput cloning and expression in recalcitrant bacteria. Nat Methods 4: 705-707.
    • (2007) Nat Methods , vol.4 , pp. 705-707
    • Geertsma, E.R.1    Poolman, B.2
  • 49
    • 23944440242 scopus 로고    scopus 로고
    • Modelling Lactococcus lactis using a genome-scale flux model
    • Oliveira AP, Nielsen J, Förster J (2005) Modelling Lactococcus lactis using a genome-scale flux model. BMC Microbiol 5: 39.
    • (2005) BMC Microbiol , vol.5 , pp. 39
    • Oliveira, A.P.1    Nielsen, J.2    Förster, J.3
  • 50
    • 34547674885 scopus 로고    scopus 로고
    • Chloroplast envelope membranes: A dynamic interface between plastids and the cytosol
    • Block MA, Douce R, Joyard J, Rolland N (2007) Chloroplast envelope membranes: a dynamic interface between plastids and the cytosol. Photosynthesis Res 92: 225-244.
    • (2007) Photosynthesis Res , vol.92 , pp. 225-244
    • Block, M.A.1    Douce, R.2    Joyard, J.3    Rolland, N.4
  • 51
    • 0017409094 scopus 로고
    • Changes in lipid composition of Escherichia coli resulting from growth with organic solvents and with food additives
    • Ingram LO (1977) Changes in lipid composition of Escherichia coli resulting from growth with organic solvents and with food additives. Appl Environ Microbiol 33: 1233-1236.
    • (1977) Appl Environ Microbiol , vol.33 , pp. 1233-1236
    • Ingram, L.O.1
  • 52
    • 0031019820 scopus 로고    scopus 로고
    • Redox chains in chloroplast envelope membranes: Spectroscopic evidence for the presence of electron carriers, including iron-sulfur centers
    • Jäger-Vottero P, Dorne AJ, Jordanov J, Douce R, Joyard J (1997) Redox chains in chloroplast envelope membranes: spectroscopic evidence for the presence of electron carriers, including iron-sulfur centers. Proc Natl Acad Sci U S A 94: 1597-1602.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 1597-1602
    • Jäger-Vottero, P.1    Dorne, A.J.2    Jordanov, J.3    Douce, R.4    Joyard, J.5
  • 53
    • 2442556067 scopus 로고    scopus 로고
    • P-type ATPase heavy metal transporters with roles in essential zinc homeostasis in Arabidopsis
    • Hussain D, Haydon MJ, Wang Y, Wong E, Sherson SM, et al. (2004) P-type ATPase heavy metal transporters with roles in essential zinc homeostasis in Arabidopsis. Plant Cell 16: 1327-1339.
    • (2004) Plant Cell , vol.16 , pp. 1327-1339
    • Hussain, D.1    Haydon, M.J.2    Wang, Y.3    Wong, E.4    Sherson, S.M.5
  • 54
    • 6344278744 scopus 로고    scopus 로고
    • Overexpression of AtHMA4 enhances root-to-shoot translocation of zinc and cadmium and plant metal tolerance
    • Verret F, Gravot A, Auroy P, Leonhardt N, David P, et al. (2004) Overexpression of AtHMA4 enhances root-to-shoot translocation of zinc and cadmium and plant metal tolerance. FEBS Lett 576: 306-312.
    • (2004) FEBS Lett , vol.576 , pp. 306-312
    • Verret, F.1    Gravot, A.2    Auroy, P.3    Leonhardt, N.4    David, P.5
  • 56
    • 66349100468 scopus 로고    scopus 로고
    • AtHMA1 contributes to the detoxification of excess Zn(II) in Arabidopsis
    • Kim YY, Choi H, Segami S, Cho HT, Martinoia E, et al. (2009) AtHMA1 contributes to the detoxification of excess Zn(II) in Arabidopsis. The Plant J 58: 737-753.
    • (2009) The Plant J , vol.58 , pp. 737-753
    • Kim, Y.Y.1    Choi, H.2    Segami, S.3    Cho, H.T.4    Martinoia, E.5
  • 57
    • 11144223456 scopus 로고    scopus 로고
    • Arabidopsis HMA2, a divalent heavy metal-transporting P(IB)-type ATPase, is involved in cytoplasmic Zn2+ homeostasis
    • Eren E, Argüello JM (2004) Arabidopsis HMA2, a divalent heavy metal-transporting P(IB)-type ATPase, is involved in cytoplasmic Zn2+ homeostasis. Plant Physiol 136: 3712-3723.
    • (2004) Plant Physiol , vol.136 , pp. 3712-3723
    • Eren, E.1    Argüello, J.M.2
  • 58
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • Toyoshima C, Nakasako M, Nomura H, Ogawa H (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405: 647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 59
  • 60
    • 33744491058 scopus 로고    scopus 로고
    • Expression in yeast and purification of a membrane protein, SERCA1a, using a biotinylated acceptor domain
    • Jidenko M, Lenoir G, Fuentes JM, le Maire M, Jaxel C (2006) Expression in yeast and purification of a membrane protein, SERCA1a, using a biotinylated acceptor domain. Protein Expr Purif 48: 32-42.
    • (2006) Protein Expr Purif , vol.48 , pp. 32-42
    • Jidenko, M.1    Lenoir, G.2    Fuentes, J.M.3    le Maire, M.4    Jaxel, C.5
  • 61
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • Le Maire M, Champeil P, Møller JV (2000) Interaction of membrane proteins and lipids with solubilizing detergents. Biochim Biophys Acta 1508: 86-111.
    • (2000) Biochim Biophys Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Møller, J.V.3
  • 62
    • 0035801906 scopus 로고    scopus 로고
    • The polar headgroup of the detergent governs the accessibility to water of tryptophan octyl ester in host micelles
    • Tortech L, Jaxel C, Vincent M, Gallay J, de Foresta B (2001) The polar headgroup of the detergent governs the accessibility to water of tryptophan octyl ester in host micelles. Biochim Biophys Acta 1514: 76-86.
    • (2001) Biochim Biophys Acta , vol.1514 , pp. 76-86
    • Tortech, L.1    Jaxel, C.2    Vincent, M.3    Gallay, J.4    de Foresta, B.5
  • 63
    • 0033567060 scopus 로고    scopus 로고
    • A comparison between the sulfhydryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochemistry
    • Getz EB, Xiao M, Chakrabarty T, Cooke R, Selvin PR (1999) A comparison between the sulfhydryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochemistry. Anal Biochem 273: 73-80.
    • (1999) Anal Biochem , vol.273 , pp. 73-80
    • Getz, E.B.1    Xiao, M.2    Chakrabarty, T.3    Cooke, R.4    Selvin, P.R.5
  • 64
    • 28844468525 scopus 로고    scopus 로고
    • Functional expression of eukaryotic membrane proteins in Lactococcus lactis
    • Monné M, Chan KW, Slotboom DJ, Kunji ERS (2005) Functional expression of eukaryotic membrane proteins in Lactococcus lactis. Protein Sci 14: 3048-3056.
    • (2005) Protein Sci , vol.14 , pp. 3048-3056
    • Monné, M.1    Chan, K.W.2    Slotboom, D.J.3    Kunji, E.R.S.4
  • 66
    • 0022367567 scopus 로고
    • Transfer of Streptococcus lactis and related streptococci to the genus Lactococcus gen. nov
    • Schleifer KH, Kraus J, Dvorak C, Kilpper-Bälz R, Collins MD, et al. (1985) Transfer of Streptococcus lactis and related streptococci to the genus Lactococcus gen. nov. Syst Appl Microbiol 6: 183-195.
    • (1985) Syst Appl Microbiol , vol.6 , pp. 183-195
    • Schleifer, K.H.1    Kraus, J.2    Dvorak, C.3    Kilpper-Bälz, R.4    Collins, M.D.5
  • 67
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant A. thaliana
    • The Arabidopsis thaliana Genome Initiative
    • The Arabidopsis thaliana Genome Initiative (2000) Analysis of the genome sequence of the flowering plant A. thaliana. Nature 408: 796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 68
    • 0041346505 scopus 로고    scopus 로고
    • Functional expression of AtHMA4, a P1B-type ATPase of the Zn/Co/Cd/Pb subclass
    • Mills RF, Krijger GC, Baccarini PJ, Hall JL, Williams LE (2003) Functional expression of AtHMA4, a P1B-type ATPase of the Zn/Co/Cd/Pb subclass. Plant J 35: 164-176.
    • (2003) Plant J , vol.35 , pp. 164-176
    • Mills, R.F.1    Krijger, G.C.2    Baccarini, P.J.3    Hall, J.L.4    Williams, L.E.5
  • 69
    • 1542328231 scopus 로고    scopus 로고
    • AtHMA3, a plant P1B ATPase, functions as a Cd/Pb transporter in yeast
    • Gravot A, Lieutaud A, Verret F, Auroy P, Vavasseur A, et al. (2004) AtHMA3, a plant P1B ATPase, functions as a Cd/Pb transporter in yeast. FEBS Lett 561: 22-28.
    • (2004) FEBS Lett , vol.561 , pp. 22-28
    • Gravot, A.1    Lieutaud, A.2    Verret, F.3    Auroy, P.4    Vavasseur, A.5
  • 70
    • 0016686551 scopus 로고
    • Improved medium for lactic streptococci and their bacteriophages
    • Terzaghi BE, Sandine WE (1975) Improved medium for lactic streptococci and their bacteriophages. Appl Environ Microbiol 29: 807-813.
    • (1975) Appl Environ Microbiol , vol.29 , pp. 807-813
    • Terzaghi, B.E.1    Sandine, W.E.2
  • 72
    • 0024345189 scopus 로고
    • High-frequency transformation, by electroporation, of Lactococcus lactis subsp. cremoris grown with glycine in osmotically stabilized media
    • Holo H, Nes IF (1989) High-frequency transformation, by electroporation, of Lactococcus lactis subsp. cremoris grown with glycine in osmotically stabilized media. Appl Environ Microbiol 55: 3119-3123.
    • (1989) Appl Environ Microbiol , vol.55 , pp. 3119-3123
    • Holo, H.1    Nes, I.F.2
  • 73
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 74
    • 0000269022 scopus 로고
    • Electrophoretic analysis of chloroplast proteins
    • Chua NH (1980) Electrophoretic analysis of chloroplast proteins. Methods Enzymol 69: 434-436.
    • (1980) Methods Enzymol , vol.69 , pp. 434-436
    • Chua, N.H.1
  • 75
    • 7044279162 scopus 로고    scopus 로고
    • Rapid one-step protein purification from plant material using the eight-amino acid StrepII epitope
    • Witte CS, Noel LD, Gielbert J, Parker JE, Romeis T (2004) Rapid one-step protein purification from plant material using the eight-amino acid StrepII epitope. Plant Mol Biol 55: 135-147.
    • (2004) Plant Mol Biol , vol.55 , pp. 135-147
    • Witte, C.S.1    Noel, L.D.2    Gielbert, J.3    Parker, J.E.4    Romeis, T.5
  • 76
    • 4143141013 scopus 로고    scopus 로고
    • Kinetic study of the enzymatic cycling reaction conducted with 3alpha-hydroxysteroid dehydrogenase in the presence of excessive thio-NAD(+) and NADH
    • Ueda S, Oda M, Imamura S, Ohnishi M (2004) Kinetic study of the enzymatic cycling reaction conducted with 3alpha-hydroxysteroid dehydrogenase in the presence of excessive thio-NAD(+) and NADH. Anal Biochem 332: 84-89.
    • (2004) Anal Biochem , vol.332 , pp. 84-89
    • Ueda, S.1    Oda, M.2    Imamura, S.3    Ohnishi, M.4
  • 77
    • 34247873159 scopus 로고    scopus 로고
    • Identification, expression, and functional analyses of a thylakoid ATP/ADP carrier from Arabidopsis
    • Thuswaldner S, Lagerstedt JO, Rojas-Stütz M, Bouhidel K, Der C, et al. (2007) Identification, expression, and functional analyses of a thylakoid ATP/ADP carrier from Arabidopsis. J Biol Chem 282: 8848-8859.
    • (2007) J Biol Chem , vol.282 , pp. 8848-8859
    • Thuswaldner, S.1    Lagerstedt, J.O.2    Rojas-Stütz, M.3    Bouhidel, K.4    Der, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.