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Volumn , Issue SUPPL.76, 2014, Pages

Expression and purification of Haemophilus influenzae rhomboid intramembrane protease GlpG for structural studies

Author keywords

Expression study; IMAC; pBAD; Rhomboid protease; SEC

Indexed keywords

PROTEINASE; RHOMBOID PROTEASE GLPG; THROMBIN; UNCLASSIFIED DRUG; PROTEINASE GLPG; BACTERIAL PROTEIN; MEMBRANE PROTEIN; RECOMBINANT PROTEIN;

EID: 84940273576     PISSN: 19343655     EISSN: 19343663     Source Type: Journal    
DOI: 10.1002/0471140864.ps2909s76     Document Type: Article
Times cited : (2)

References (44)
  • 1
    • 40049099087 scopus 로고    scopus 로고
    • Microscale fluorescent thermal stability assay for membrane proteins
    • Alexandrov, A.I., Mileni, M., Chien, E.Y., Hanson, M.A., and Stevens, R.C. 2008. Microscale fluorescent thermal stability assay for membrane proteins. Structure 16:351-359.
    • (2008) Structure , vol.16 , pp. 351-359
    • Alexandrov, A.I.1    Mileni, M.2    Chien, E.Y.3    Hanson, M.A.4    Stevens, R.C.5
  • 2
    • 0035810954 scopus 로고    scopus 로고
    • High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter
    • Auer, M., Kim, M.J., Lemieux, M.J., Villa, A., Song, J., Li, X.D., and Wang, D.N. 2001. High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter. Biochemistry 40:6628-6635.
    • (2001) Biochemistry , vol.40 , pp. 6628-6635
    • Auer, M.1    Kim, M.J.2    Lemieux, M.J.3    Villa, A.4    Song, J.5    Li, X.D.6    Wang, D.N.7
  • 3
    • 33846275257 scopus 로고    scopus 로고
    • Structural basis for intramembrane proteolysis by rhomboid serine proteases
    • Ben-Shem, A., Fass, D., and Bibi, E. 2007. Structural basis for intramembrane proteolysis by rhomboid serine proteases. Proc. Natl. Acad. Sci. U.S.A. 104:462-466.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 462-466
    • Ben-Shem, A.1    Fass, D.2    Bibi, E.3
  • 5
    • 0027347272 scopus 로고
    • Analysis of membrane proteins by western blotting and enhanced chemiluminescence
    • Bradd, S. J. and Dunn, M. J. 1993. Analysis of membrane proteins by western blotting and enhanced chemiluminescence. Methods Mol. Biol. 19:211-218
    • (1993) Methods Mol. Biol. , vol.19 , pp. 211-218
    • Bradd, S.J.1    Dunn, M.J.2
  • 7
    • 84878269745 scopus 로고    scopus 로고
    • Rapid expression screening of eukaryotic membrane proteins in Pichia pastoris
    • Brooks, C.L., Morisson, M.A., and Lemieux, M.J. 2013. Rapid expression screening of eukaryotic membrane proteins in Pichia pastoris. Protein Sci. 22:425-433.
    • (2013) Protein Sci. , vol.22 , pp. 425-433
    • Brooks, C.L.1    Morisson, M.A.2    Lemieux, M.J.3
  • 8
    • 0037071906 scopus 로고    scopus 로고
    • Construction and deconstruction of bacterial inclusion bodies
    • Carrio, M.M. andVillaverde, A. 2002. Construction and deconstruction of bacterial inclusion bodies. J. Biotechnol. 96:3-12.
    • (2002) J. Biotechnol. , vol.96 , pp. 3-12
    • Carrio, M.M.1    Villaverde, A.2
  • 9
    • 0346935999 scopus 로고    scopus 로고
    • DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli
    • Chen, Y., Song, J., Sui, S.F., and Wang, D.N. 2003. DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli. Protein Expr. Purif. 32: 221-231.
    • (2003) Protein Expr. Purif. , vol.32 , pp. 221-231
    • Chen, Y.1    Song, J.2    Sui, S.F.3    Wang, D.N.4
  • 10
    • 84862803226 scopus 로고    scopus 로고
    • Identification and characterization of a bacterial hydrosulphide ion channel
    • Czyzewski, B.K. and Wang, D.N. 2012. Identification and characterization of a bacterial hydrosulphide ion channel. Nature 483:494-497.
    • (2012) Nature , vol.483 , pp. 494-497
    • Czyzewski, B.K.1    Wang, D.N.2
  • 11
    • 0037240246 scopus 로고    scopus 로고
    • A rapid method for assessing lipid: Protein and detergent: Protein ratios in membrane-protein crystallization
    • DaCosta, C.J.B. and Baenziger, J.E. 2002. A rapid method for assessing lipid: Protein and detergent: Protein ratios in membrane-protein crystallization. Acta Crystallogr. DBiol. Crystallogr. 59:77-83.
    • (2002) Acta Crystallogr. DBiol. Crystallogr. , vol.59 , pp. 77-83
    • DaCosta, C.J.B.1    Baenziger, J.E.2
  • 12
    • 84858407937 scopus 로고    scopus 로고
    • Oligomeric status and nucleotide binding properties of the plastid ATP/ADP transporter 1: Toward a molecular understanding of the transport mechanism
    • Deniaud, A., Panwar, P., Frelet-Barrand, A., Bernaudat, F., Juillan-Binard, C., Ebel, C., Rolland, N., and Pebay-Peyroula, E. 2012. Oligomeric status and nucleotide binding properties of the plastid ATP/ADP transporter 1: Toward a molecular understanding of the transport mechanism. PloS One 7:e32325.
    • (2012) PloS One , vol.7
    • Deniaud, A.1    Panwar, P.2    Frelet-Barrand, A.3    Bernaudat, F.4    Juillan-Binard, C.5    Ebel, C.6    Rolland, N.7    Pebay-Peyroula, E.8
  • 13
    • 0028907619 scopus 로고
    • Gratuitous overexpression of genes in Escherichia coli leads to growth inhibition and ribosome destruction
    • Dong, H., Nilsson, L., andKurland, C.G. 1995. Gratuitous overexpression of genes in Escherichia coli leads to growth inhibition and ribosome destruction. J. Bacteriol. 177:1497-1504.
    • (1995) J. Bacteriol. , vol.177 , pp. 1497-1504
    • Dong, H.1    Nilsson, L.2    Kurland, C.G.3
  • 14
    • 43149098999 scopus 로고    scopus 로고
    • GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae
    • Drew, D., Newstead, S., Sonoda, Y., Kim, H., von Heijne, G., and Iwata, S. 2008. GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae. Nat. Protoc. 3:784-798.
    • (2008) Nat. Protoc. , vol.3 , pp. 784-798
    • Drew, D.1    Newstead, S.2    Sonoda, Y.3    Kim, H.4    von Heijne, G.5    Iwata, S.6
  • 15
    • 58549108805 scopus 로고    scopus 로고
    • Rhomboid proteases and their biological functions
    • Freeman, M. 2008. Rhomboid proteases and their biological functions. Annu. Rev. Genet. 42:191-210.
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 191-210
    • Freeman, M.1
  • 16
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L.M., Belin, D., Carson, M.J., and Beckwith, J. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 17
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang, Y., Lemieux, M.J., Song, J., Auer, M., and Wang, D.N. 2003. Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301:616-620.
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 18
    • 33646011258 scopus 로고    scopus 로고
    • Fluorescencedetection size-exclusion chromatography for precrystallization screening of integral membrane proteins
    • Kawate, T. and Gouaux, E. 2006. Fluorescencedetection size-exclusion chromatography for precrystallization screening of integral membrane proteins. Structure 14:673-681.
    • (2006) Structure , vol.14 , pp. 673-681
    • Kawate, T.1    Gouaux, E.2
  • 19
    • 84875223117 scopus 로고    scopus 로고
    • Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease
    • Lazareno-Saez, C., Arutyunova, E., Coquelle, N., and Lemieux, M.J. 2013. Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease. J. Mol. Biol. 425:1127-1142.
    • (2013) J. Mol. Biol. , vol.425 , pp. 1127-1142
    • Lazareno-Saez, C.1    Arutyunova, E.2    Coquelle, N.3    Lemieux, M.J.4
  • 20
    • 0036427425 scopus 로고    scopus 로고
    • Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain
    • Lemieux, M.J., Reithmeier, R.A., and Wang, D.N. 2002. Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain. J. Struct. Biol. 137:322-332.
    • (2002) J. Struct. Biol. , vol.137 , pp. 322-332
    • Lemieux, M.J.1    Reithmeier, R.A.2    Wang, D.N.3
  • 21
    • 0345276579 scopus 로고    scopus 로고
    • Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: A member of the major facilitator superfamily
    • Lemieux, M.J., Song, J., Kim, M.J., Huang, Y., Villa, A., Auer, M., Li, X.D., and Wang, D.N. 2003. Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: A member of the major facilitator superfamily. Protein Sci. 12:2748-2756.
    • (2003) Protein Sci. , vol.12 , pp. 2748-2756
    • Lemieux, M.J.1    Song, J.2    Kim, M.J.3    Huang, Y.4    Villa, A.5    Auer, M.6    Li, X.D.7    Wang, D.N.8
  • 22
    • 33846543356 scopus 로고    scopus 로고
    • The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis
    • Lemieux, M.J., Fischer, S.J., Cherney, M.M., Bateman, K.S., and James, M.N. 2007. The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis. Proc. Natl. Acad. Sci. U.S.A. 104:750-754.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 750-754
    • Lemieux, M.J.1    Fischer, S.J.2    Cherney, M.M.3    Bateman, K.S.4    James, M.N.5
  • 25
    • 84869884515 scopus 로고    scopus 로고
    • Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter
    • Mancusso, R., Gregorio, G.G., Liu, Q., and Wang, D.N. 2012. Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter. Nature 491:622-626.
    • (2012) Nature , vol.491 , pp. 622-626
    • Mancusso, R.1    Gregorio, G.G.2    Liu, Q.3    Wang, D.N.4
  • 26
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli:Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B. andWalker, J.E. 1996. Over-production of proteins in Escherichia coli:Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:289-298.
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 27
    • 0842288662 scopus 로고    scopus 로고
    • Membrane protein expression and production: Effects of polyhistidine tag length and position
    • Mohanty, A.K. andWiener, M.C. 2004. Membrane protein expression and production: Effects of polyhistidine tag length and position. Protein H. influenzae Expr. Purif. 33:311-325.
    • (2004) Protein H. influenzae Expr. Purif. , vol.33 , pp. 311-325
    • Mohanty, A.K.1    Wiener, M.C.2
  • 28
    • 78650798464 scopus 로고    scopus 로고
    • Restrained expression, a method to overproduce toxicmembrane proteins by exploiting operatorrepressor interactions
    • Narayanan, A., Ridilla, M., andYernool, D.A. 2011. Restrained expression, a method to overproduce toxicmembrane proteins by exploiting operatorrepressor interactions. Protein Sci. 20:51-61.
    • (2011) Protein Sci. , vol.20 , pp. 51-61
    • Narayanan, A.1    Ridilla, M.2    Yernool, D.A.3
  • 29
    • 80052008858 scopus 로고    scopus 로고
    • Improving recombinant eukaryotic membrane protein yields in Pichia pastoris: The importance of codon optimization and clone selection
    • Oberg, F., Sjohamn, J., Conner, M.T., Bill, R.M., and Hedfalk, K. 2011. Improving recombinant eukaryotic membrane protein yields in Pichia pastoris: The importance of codon optimization and clone selection. Mol. Membr. Biol. 28:398-411.
    • (2011) Mol. Membr. Biol. , vol.28 , pp. 398-411
    • Oberg, F.1    Sjohamn, J.2    Conner, M.T.3    Bill, R.M.4    Hedfalk, K.5
  • 30
    • 78751683949 scopus 로고    scopus 로고
    • The morphology and composition of cholesterol-rich micellar nanostructures determine transmembrane protein (GPCR) activity
    • O'Malley, M.A., Helgeson, M.E., Wagner, N.J., and Robinson, A.S. 2011. The morphology and composition of cholesterol-rich micellar nanostructures determine transmembrane protein (GPCR) activity. Biophys. J. 100: 11-13.
    • (2011) Biophys. J. , vol.100 , pp. 11-13
    • O'Malley, M.A.1    Helgeson, M.E.2    Wagner, N.J.3    Robinson, A.S.4
  • 31
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • Porath, J., Carlsson, J., Olsson, I., and Belfrage, G. 1975. Metal chelate affinity chromatography, a new approach to protein fractionation. Nature 258:598-599.
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 32
    • 84864131010 scopus 로고    scopus 로고
    • Sizeexclusion chromatography with multi-angle light scattering for elucidating protein aggregation mechanisms
    • Sahin, E. and Roberts, C.J. 2012. Sizeexclusion chromatography with multi-angle light scattering for elucidating protein aggregation mechanisms. Methods Mol. Biol. 899: 403-423.
    • (2012) Methods Mol. Biol. , vol.899 , pp. 403-423
    • Sahin, E.1    Roberts, C.J.2
  • 34
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids and detergents: Not just a soap opera
    • Seddon, A.M., Curnow, P., and Booth, P.J. 2004. Membrane proteins, lipids and detergents: Not just a soap opera. Biochim. Biophys. Acta 1666:105-117.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 35
    • 38949158505 scopus 로고    scopus 로고
    • Conformational thermostabilization of the beta1-adrenergic receptor in a detergent-resistant form
    • Serrano-Vega, M.J., Magnani, F., Shibata, Y., and Tate, C.G. 2008. Conformational thermostabilization of the beta1-adrenergic receptor in a detergent-resistant form. Proc. Natl. Acad. Sci. U.S.A. 105:877-882.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 877-882
    • Serrano-Vega, M.J.1    Magnani, F.2    Shibata, Y.3    Tate, C.G.4
  • 37
    • 77950496251 scopus 로고    scopus 로고
    • Practical considerations of membrane protein instability during purification and crystallisation
    • Tate, C.G. 2010. Practical considerations of membrane protein instability during purification and crystallisation. Methods Mol. Biol. 601:187-203.
    • (2010) Methods Mol. Biol. , vol.601 , pp. 187-203
    • Tate, C.G.1
  • 40
    • 1542464748 scopus 로고    scopus 로고
    • Purification and characterization of transporter proteins from human erythrocyte membrane
    • Wang, D.N., Lemieux, M.J., and Boulter, J.M. 2003. Purification and characterization of transporter proteins from human erythrocyte membrane. Methods Mol. Biol. 228:239-255.
    • (2003) Methods Mol. Biol. , vol.228 , pp. 239-255
    • Wang, D.N.1    Lemieux, M.J.2    Boulter, J.M.3
  • 41
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Wang, Y., Zhang, Y., and Ha, Y. 2006. Crystal structure of a rhomboid family intramembrane protease. Nature 444:179-180.
    • (2006) Nature , vol.444 , pp. 179-180
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 42
    • 4344579363 scopus 로고    scopus 로고
    • A pedestrian guide to membrane protein crystallization
    • Wiener, M.C. 2004. A pedestrian guide to membrane protein crystallization. Methods 34:364-372.
    • (2004) Methods , vol.34 , pp. 364-372
    • Wiener, M.C.1
  • 44
    • 34548684744 scopus 로고    scopus 로고
    • LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake
    • Zhou, Z., Zhen, J., Karpowich, N.K., Goetz, R.M., Law, C.J., Reith, M.E., and Wang, D.N. 2007. LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake. Science 317:1390-1393.
    • (2007) Science , vol.317 , pp. 1390-1393
    • Zhou, Z.1    Zhen, J.2    Karpowich, N.K.3    Goetz, R.M.4    Law, C.J.5    Reith, M.E.6    Wang, D.N.7


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