메뉴 건너뛰기




Volumn 5, Issue 3, 1996, Pages 456-467

Overexpression of bacterio-opsin in Escherichia coli as a water-soluble fusion to maltose binding protein: Efficient regeneration of the fusion protein and selective cleavage with trypsin

Author keywords

bacteriorhodopsin; Escherichia coli; maltose binding protein; membrane protein overexpression; membrane protein refolding; selective trypsin cleavage; synthetic gene

Indexed keywords

BACTERIORHODOPSIN; HYBRID PROTEIN; MALTOSE BINDING PROTEIN;

EID: 0030001914     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050307     Document Type: Article
Times cited : (40)

References (52)
  • 2
    • 0026640605 scopus 로고
    • In vitro synthesis of bacterio-opsin: Integration into microsomal membranes
    • Bauer U, Hildebrandt V, Dencher NA, Wrede P. 1992. In vitro synthesis of bacterio-opsin: Integration into microsomal membranes. Biochem Biophys Res Commun 187:1480-1485.
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 1480-1485
    • Bauer, U.1    Hildebrandt, V.2    Dencher, N.A.3    Wrede, P.4
  • 4
    • 0023645168 scopus 로고
    • Structure-function studies on bacteriorhodopsin. IV. Purification and renaturation of bacterio-opsin polypeptide expressed in Escherichia coli
    • Braiman MS, Stern LJ, Chao BH, Khorana HG. 1987. Structure-function studies on bacteriorhodopsin. IV. Purification and renaturation of bacterio-opsin polypeptide expressed in Escherichia coli. J Biol Chem 262:9271-9276.
    • (1987) J Biol Chem , vol.262 , pp. 9271-9276
    • Braiman, M.S.1    Stern, L.J.2    Chao, B.H.3    Khorana, H.G.4
  • 5
    • 0027947674 scopus 로고
    • Total gene synthesis: Novel single-step and convergent strategies applied to the construction of a 779 base pair bacteriorhodopsin gene
    • Chen GQ, Choi I, Ramachandran B, Gouaux JE. 1994. Total gene synthesis: Novel single-step and convergent strategies applied to the construction of a 779 base pair bacteriorhodopsin gene. J Am Chem Soc 116: 8799-8800.
    • (1994) J Am Chem Soc , vol.116 , pp. 8799-8800
    • Chen, G.Q.1    Choi, I.2    Ramachandran, B.3    Gouaux, J.E.4
  • 6
    • 0020007210 scopus 로고
    • Purification of bovine rhodopsin over concanavalin A-Sepharose
    • De Grip WJ. 1982. Purification of bovine rhodopsin over concanavalin A-Sepharose. Methods Enzymol 81:197-201.
    • (1982) Methods Enzymol , vol.81 , pp. 197-201
    • De Grip, W.J.1
  • 7
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J, Haeberli P, Smithies O. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12:387-395.
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 8
    • 0027536538 scopus 로고
    • Homologous bacterio-opsin-encoding gene expression via site-specific vector integration
    • Ferrando E, Schweiger U, Oesterhelt D. 1993. Homologous bacterio-opsin-encoding gene expression via site-specific vector integration. Gene 125:41-47.
    • (1993) Gene , vol.125 , pp. 41-47
    • Ferrando, E.1    Schweiger, U.2    Oesterhelt, D.3
  • 9
    • 0029037099 scopus 로고
    • Isolated RNA binding domain of a class I tRNA synthetase
    • Gale AJ, Schimmel P. 1995. Isolated RNA binding domain of a class I tRNA synthetase. Biochemistry 34:8896-8903.
    • (1995) Biochemistry , vol.34 , pp. 8896-8903
    • Gale, A.J.1    Schimmel, P.2
  • 10
    • 0027361998 scopus 로고
    • Expression of a rat neurotensin receptor in Escherichia coli
    • Grisshammer R, Duckworth R, Henderson R. 1993. Expression of a rat neurotensin receptor in Escherichia coli. Biochem J 295:571-576.
    • (1993) Biochem J , vol.295 , pp. 571-576
    • Grisshammer, R.1    Duckworth, R.2    Henderson, R.3
  • 11
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R, Baldwin JM, Ceska TA, Zemlin F, Beckmann E, Downing KH. 1990. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol 213:899-929.
    • (1990) J Mol Biol , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 12
    • 84989742197 scopus 로고
    • Purple fission yeast: Over-expression and processing of the pigment bacteriorhodopsin in Schizosaccharomyces pombe
    • Hildebrandt V, Polakowski F, Buldt G. 1991. Purple fission yeast: Over-expression and processing of the pigment bacteriorhodopsin in Schizosaccharomyces pombe. Photochem Photobiol 54:1009-1016.
    • (1991) Photochem Photobiol , vol.54 , pp. 1009-1016
    • Hildebrandt, V.1    Polakowski, F.2    Buldt, G.3
  • 14
    • 0242285207 scopus 로고
    • Delipidation of bacteriorhodopsin and reconstitution with exogenous phospholipid
    • Huang KS, Bayley H, Khorana HG. 1980. Delipidation of bacteriorhodopsin and reconstitution with exogenous phospholipid. Proc Natl Acad Sci USA 77:323-327.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 323-327
    • Huang, K.S.1    Bayley, H.2    Khorana, H.G.3
  • 15
    • 0019887931 scopus 로고
    • Refolding of an integral membrane protein. Denaturation, renaturation and reconstitution of intact bacteriorhodopsin and two proteolytic fragments
    • Huang KS, Bayley H, Liao MJ, London E, Khorana HG. 1981. Refolding of an integral membrane protein. Denaturation, renaturation and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. J Biol Chem 256:3802-3809.
    • (1981) J Biol Chem , vol.256 , pp. 3802-3809
    • Huang, K.S.1    Bayley, H.2    Liao, M.J.3    London, E.4    Khorana, H.G.5
  • 16
    • 0026642866 scopus 로고
    • Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment
    • Kahn TW, Engelman DM. 1992. Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment. Biochemistry 51:6144-6151.
    • (1992) Biochemistry , vol.51 , pp. 6144-6151
    • Kahn, T.W.1    Engelman, D.M.2
  • 18
    • 0020347668 scopus 로고
    • Maltose binding protein from Escherichia coli
    • Kellermann OK, Ferenci T. 1982. Maltose binding protein from Escherichia coli. Methods Enzymol 90:459-463.
    • (1982) Methods Enzymol , vol.90 , pp. 459-463
    • Kellermann, O.K.1    Ferenci, T.2
  • 19
    • 0027394224 scopus 로고
    • Two light-transducing membrane proteins: Bacteriorhodopsin and the mammalian rhodopsin
    • Khorana HG. 1993. Two light-transducing membrane proteins: Bacteriorhodopsin and the mammalian rhodopsin. Proc Natl Acad Sci USA 90:1166-1171.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1166-1171
    • Khorana, H.G.1
  • 21
    • 0027524866 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator
    • Ko YH, Thomas PJ, Delannoy MR, Pedersen PL. 1993. The cystic fibrosis transmembrane conductance regulator. J Biol Chem 268:24330-24338.
    • (1993) J Biol Chem , vol.268 , pp. 24330-24338
    • Ko, Y.H.1    Thomas, P.J.2    Delannoy, M.R.3    Pedersen, P.L.4
  • 23
    • 0027526352 scopus 로고
    • Mechanism of light-dependent proton translocation by bacteriorhodopsin
    • Krebs MP, Khorana HG. 1993. Mechanism of light-dependent proton translocation by bacteriorhodopsin. J Bacteriol 175:1555-1560.
    • (1993) J Bacteriol , vol.175 , pp. 1555-1560
    • Krebs, M.P.1    Khorana, H.G.2
  • 24
    • 0027769837 scopus 로고
    • Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin
    • Lanyi JK. 1993. Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin. Biochim Biophys Acta 1183:241-261.
    • (1993) Biochim Biophys Acta , vol.1183 , pp. 241-261
    • Lanyi, J.K.1
  • 25
    • 0021112513 scopus 로고
    • Regeneration of the native bacteriorhodopsin structure from two chymotryptic fragments
    • Liao MJ, London E, Khorana HG. 1983. Regeneration of the native bacteriorhodopsin structure from two chymotryptic fragments. J Biol Chem 258:9949-9955.
    • (1983) J Biol Chem , vol.258 , pp. 9949-9955
    • Liao, M.J.1    London, E.2    Khorana, H.G.3
  • 26
    • 0020490831 scopus 로고
    • Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures
    • London E, Khorana HG. 1982. Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures. J Biol Chem 257: 7003-7011.
    • (1982) J Biol Chem , vol.257 , pp. 7003-7011
    • London, E.1    Khorana, H.G.2
  • 27
    • 0021766626 scopus 로고
    • Localization of binding sites for carboxyl terminal specific anti-rhodopsin monoclonal antibodies using synthetic peptides
    • MacKenzie D, Arendt A, Hargrave P, McDowell JH, Molday RS. 1984. Localization of binding sites for carboxyl terminal specific anti-rhodopsin monoclonal antibodies using synthetic peptides. Biochemistry 23:6544-6549.
    • (1984) Biochemistry , vol.23 , pp. 6544-6549
    • MacKenzie, D.1    Arendt, A.2    Hargrave, P.3    McDowell, J.H.4    Molday, R.S.5
  • 29
    • 0025829307 scopus 로고
    • From femtoseconds to biology: Mechanism of bacteriorhodopsin's light-driven proton pump
    • Mathies RA, Lin SW, Ames JB, Pollard WT. 1991. From femtoseconds to biology: Mechanism of bacteriorhodopsin's light-driven proton pump. Annu Rev Biophys Biophys Chem 20:491-518.
    • (1991) Annu Rev Biophys Biophys Chem , vol.20 , pp. 491-518
    • Mathies, R.A.1    Lin, S.W.2    Ames, J.B.3    Pollard, W.T.4
  • 30
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidine difluoride membranes
    • Matsudaira P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidine difluoride membranes. J Biol Chem 262: 10035-10038.
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 31
    • 0025727680 scopus 로고
    • Wild-type and mutant bacteriorhodopsins D85N, D96N, and R82Q: Purification to homogeneity, pH dependence of pumping, and electron diffraction
    • Miercke LJW, Betlach MC, Mitra AK, Shand RF, Fong SK, Stroud RM. 1991. Wild-type and mutant bacteriorhodopsins D85N, D96N, and R82Q: Purification to homogeneity, pH dependence of pumping, and electron diffraction. Biochemistry 30:3088-3098.
    • (1991) Biochemistry , vol.30 , pp. 3088-3098
    • Miercke, L.J.W.1    Betlach, M.C.2    Mitra, A.K.3    Shand, R.F.4    Fong, S.K.5    Stroud, R.M.6
  • 32
    • 0025731582 scopus 로고
    • Effects of detergent environments on the photocycle of purified monomeric bacteriorhodopsin
    • Milder SJ, Thorgeirsson TE, Miercke LJW, Stroud RM, Kliger DS. 1991. Effects of detergent environments on the photocycle of purified monomeric bacteriorhodopsin. Biochemistry 30:1751-1761.
    • (1991) Biochemistry , vol.30 , pp. 1751-1761
    • Milder, S.J.1    Thorgeirsson, T.E.2    Miercke, L.J.W.3    Stroud, R.M.4    Kliger, D.S.5
  • 33
    • 0021890938 scopus 로고
    • Isolation of detergent-solubilized monomers of bacteriorhodopsin by size-exclusion high-performance liquid chromatography
    • Muccio DD, DeLucas LJ. 1985. Isolation of detergent-solubilized monomers of bacteriorhodopsin by size-exclusion high-performance liquid chromatography. J Chromatography 326:243-250.
    • (1985) J Chromatography , vol.326 , pp. 243-250
    • Muccio, D.D.1    DeLucas, L.J.2
  • 35
    • 0025303033 scopus 로고
    • An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium
    • Ni B, Chang M, Duschl A, Lanyi J, Needleman R. 1990. An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium. Gene 90:169-172
    • (1990) Gene , vol.90 , pp. 169-172
    • Ni, B.1    Chang, M.2    Duschl, A.3    Lanyi, J.4    Needleman, R.5
  • 36
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt D, Stoeckenius W 1971. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature New Biology 233:149-152.
    • (1971) Nature New Biology , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 39
    • 0027535568 scopus 로고
    • High-yield production of bacteriorhodopsin via expression of a synthetic gene in Escherichia coli
    • Pompejus M, Friedrich K, Teufel M, Fritz HJ. 1993. High-yield production of bacteriorhodopsin via expression of a synthetic gene in Escherichia coli. Eur J Biochem 211:27-35.
    • (1993) Eur J Biochem , vol.211 , pp. 27-35
    • Pompejus, M.1    Friedrich, K.2    Teufel, M.3    Fritz, H.J.4
  • 40
    • 0027050148 scopus 로고
    • Recursive PCR: A novel technique for total gene synthesis
    • Prodromou C, Pearl LH. 1992. Recursive PCR: A novel technique for total gene synthesis. Protein Eng 5:827-829.
    • (1992) Protein Eng , vol.5 , pp. 827-829
    • Prodromou, C.1    Pearl, L.H.2
  • 41
    • 0024338686 scopus 로고
    • Expression in Escherichia coli of fragments of glial fibrillary acidic protein: Characterization, assembly properties and paracrystal formation
    • Quinlan RA, Moir RD, Stewart M. 1989. Expression in Escherichia coli of fragments of glial fibrillary acidic protein: Characterization, assembly properties and paracrystal formation J Cell Sci 93:71-83.
    • (1989) J Cell Sci , vol.93 , pp. 71-83
    • Quinlan, R.A.1    Moir, R.D.2    Stewart, M.3
  • 42
    • 0018805369 scopus 로고
    • Binding of all-trans-retinal to the purple membrane. Evidence for cooperativity and determination of the extinction coefficient
    • Rehorek M, Heyn MP. 1979. Binding of all-trans-retinal to the purple membrane. Evidence for cooperativity and determination of the extinction coefficient Biochemistry 18:4977-4983.
    • (1979) Biochemistry , vol.18 , pp. 4977-4983
    • Rehorek, M.1    Heyn, M.P.2
  • 45
    • 0026502381 scopus 로고
    • Dual asymmetric PCR: One-step construction of synthetic genes
    • Sandhu GS, Aleff RA, Kline BC. 1992. Dual asymmetric PCR: One-step construction of synthetic genes. BioTechniques 12:14-16.
    • (1992) BioTechniques , vol.12 , pp. 14-16
    • Sandhu, G.S.1    Aleff, R.A.2    Kline, B.C.3
  • 46
    • 0001751353 scopus 로고
    • Overproduction of membrane proteins
    • Schertler GFX 1992. Overproduction of membrane proteins. Curr Op Struct Biol 2:534-544.
    • (1992) Curr Op Struct Biol , vol.2 , pp. 534-544
    • Schertler, G.F.X.1
  • 47
    • 0025804937 scopus 로고
    • Wild-type and mutant bacterioopsins D85N, D96N, and R82Q: High-level expression in Escherichia coli
    • Shand RF, Miercke LJW, Mitra AK, Fong SK, Stroud RM, Betlach MC. 1991. Wild-type and mutant bacterioopsins D85N, D96N, and R82Q: High-level expression in Escherichia coli. Biochemistry 30:3082-3088.
    • (1991) Biochemistry , vol.30 , pp. 3082-3088
    • Shand, R.F.1    Miercke, L.J.W.2    Mitra, A.K.3    Fong, S.K.4    Stroud, R.M.5    Betlach, M.C.6
  • 48
    • 0027772177 scopus 로고
    • Cell-free synthesis, functional refolding, and spectroscopic characterization of bacteriorhodopsin, an integral membrane protein
    • Sonar S, Patel N, Fischer W, Rothschild KJ. 1993. Cell-free synthesis, functional refolding, and spectroscopic characterization of bacteriorhodopsin, an integral membrane protein. Biochemistry 32:13777-13781.
    • (1993) Biochemistry , vol.32 , pp. 13777-13781
    • Sonar, S.1    Patel, N.2    Fischer, W.3    Rothschild, K.J.4
  • 49
    • 0000073823 scopus 로고
    • The molar extinction of rhodopsin
    • Wald G, Brown PK. 1953. The molar extinction of rhodopsin. J Gen Physiol 37:189-200.
    • (1953) J Gen Physiol , vol.37 , pp. 189-200
    • Wald, G.1    Brown, P.K.2
  • 50
    • 0017577095 scopus 로고
    • The preparation of lipid-depleted bacteriorhodopsin
    • Wildenauer D, Khorana HG. 1977. The preparation of lipid-depleted bacteriorhodopsin. Biochim Biophys Acta 466:315-324.
    • (1977) Biochim Biophys Acta , vol.466 , pp. 315-324
    • Wildenauer, D.1    Khorana, H.G.2
  • 51
    • 0027164153 scopus 로고
    • Visualization of the morphology of purple membrane surfaces by monoclonal antibody techniques
    • Yamaguchi N, Jinbo Y, Arai M, Koyama K. 1993 Visualization of the morphology of purple membrane surfaces by monoclonal antibody techniques. FEBS Lett 324:287-292.
    • (1993) FEBS Lett , vol.324 , pp. 287-292
    • Yamaguchi, N.1    Jinbo, Y.2    Arai, M.3    Koyama, K.4
  • 52
    • 0026674106 scopus 로고
    • Gene synthesis and expression in E. coli for PUMP, a human matrix metalloproteinase
    • Ye QZ, Johnson LL, Baragi V. 1992. Gene synthesis and expression in E. coli for PUMP, a human matrix metalloproteinase. Biochem Biophys Res Commun 186:143-149.
    • (1992) Biochem Biophys Res Commun , vol.186 , pp. 143-149
    • Ye, Q.Z.1    Johnson, L.L.2    Baragi, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.