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Volumn 1778, Issue 5, 2008, Pages 1237-1250

High yield cell-free production of integral membrane proteins without refolding or detergents

Author keywords

Cell free protein synthesis; In vitro protein synthesis; Integral membrane protein; Transporter

Indexed keywords

CELL EXTRACT; INTEGRAL MEMBRANE PROTEIN; MANNITOL PERMEASE; MEMBRANE PROTEIN; PERMEASE; PROTEINASE; SUCROSE; TETRACYCLINE PUMP;

EID: 43049142194     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.01.023     Document Type: Article
Times cited : (96)

References (60)
  • 2
    • 0037450542 scopus 로고    scopus 로고
    • Assembly and overexpression of membrane proteins in Escherichia coli
    • Drew D., Froderberg L., Baars L., and de Gier J.W. Assembly and overexpression of membrane proteins in Escherichia coli. Biochim. Biophys. Acta 1610 (2003) 3-10
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 3-10
    • Drew, D.1    Froderberg, L.2    Baars, L.3    de Gier, J.W.4
  • 3
    • 0037450574 scopus 로고    scopus 로고
    • Practical aspects of overexpressing bacterial secondary membrane transporters for structural studies
    • Wang D.N., Safferling M., Lemieux M.J., Griffith H., Chen Y., and Li X.D. Practical aspects of overexpressing bacterial secondary membrane transporters for structural studies. Biochim. Biophys. Acta 1610 (2003) 23-36
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 23-36
    • Wang, D.N.1    Safferling, M.2    Lemieux, M.J.3    Griffith, H.4    Chen, Y.5    Li, X.D.6
  • 4
    • 14144256100 scopus 로고    scopus 로고
    • An efficient strategy for high-throughput expression screening of recombinant integral membrane proteins
    • Eshaghi S., Hedren M., Nasser M.I.A., Hammarberg T., Thornell A., and Nordlund P. An efficient strategy for high-throughput expression screening of recombinant integral membrane proteins. Protein Sci. 14 (2005) 676-683
    • (2005) Protein Sci. , vol.14 , pp. 676-683
    • Eshaghi, S.1    Hedren, M.2    Nasser, M.I.A.3    Hammarberg, T.4    Thornell, A.5    Nordlund, P.6
  • 5
    • 0037450517 scopus 로고    scopus 로고
    • In vitro folding of alpha-helical membrane proteins
    • Kiefer H. In vitro folding of alpha-helical membrane proteins. Biochim. Biophys. Acta 1610 (2003) 57-62
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 57-62
    • Kiefer, H.1
  • 6
    • 0037450548 scopus 로고    scopus 로고
    • The expression of outer membrane proteins for crystallization
    • Bannwarth M., and Schulz G.E. The expression of outer membrane proteins for crystallization. Biochim. Biophys. Acta 1610 (2003) 37-45
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 37-45
    • Bannwarth, M.1    Schulz, G.E.2
  • 8
    • 33748307399 scopus 로고    scopus 로고
    • Cell-free expression as an emerging technique for the large scale production of integral membrane protein
    • Klammt C., Schwarz D., Lohr F., Schneider B., Dotsch V., and Bernhard F. Cell-free expression as an emerging technique for the large scale production of integral membrane protein. FEBS J. 273 (2006) 4141-4153
    • (2006) FEBS J. , vol.273 , pp. 4141-4153
    • Klammt, C.1    Schwarz, D.2    Lohr, F.3    Schneider, B.4    Dotsch, V.5    Bernhard, F.6
  • 9
    • 29344450131 scopus 로고    scopus 로고
    • X-ray structure of the EmrE multidrug transporter in complex with a substrate
    • Pornillos O., Chen Y.J., Chen A.P., and Chang G. X-ray structure of the EmrE multidrug transporter in complex with a substrate. Science 310 (2005) 1950-1953
    • (2005) Science , vol.310 , pp. 1950-1953
    • Pornillos, O.1    Chen, Y.J.2    Chen, A.P.3    Chang, G.4
  • 10
    • 15744391469 scopus 로고    scopus 로고
    • Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors
    • Ishihara G., Goto M., Saeki M., Ito K., Hori T., Kigawa T., Shirouzu M., and Yokoyama S. Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors. Protein Expr. Purif. 41 (2005) 27-37
    • (2005) Protein Expr. Purif. , vol.41 , pp. 27-37
    • Ishihara, G.1    Goto, M.2    Saeki, M.3    Ito, K.4    Hori, T.5    Kigawa, T.6    Shirouzu, M.7    Yokoyama, S.8
  • 12
    • 0033520449 scopus 로고    scopus 로고
    • Cell-free expression and functional reconstitution of homo-oligomeric alpha7 nicotinic acetylcholine receptors into planar lipid bilayers
    • Lyford L.K., and Rosenberg R.L. Cell-free expression and functional reconstitution of homo-oligomeric alpha7 nicotinic acetylcholine receptors into planar lipid bilayers. J. Biol. Chem. 274 (1999) 25675-25681
    • (1999) J. Biol. Chem. , vol.274 , pp. 25675-25681
    • Lyford, L.K.1    Rosenberg, R.L.2
  • 13
    • 0031035737 scopus 로고    scopus 로고
    • Membrane insertion, glycosylation, and oligomerization of inositol trisphosphate receptors in a cell-free translation system
    • Joseph S.K., Boehning D., Pierson S., and Nicchitta C.V. Membrane insertion, glycosylation, and oligomerization of inositol trisphosphate receptors in a cell-free translation system. J. Biol. Chem. 272 (1997) 1579-1588
    • (1997) J. Biol. Chem. , vol.272 , pp. 1579-1588
    • Joseph, S.K.1    Boehning, D.2    Pierson, S.3    Nicchitta, C.V.4
  • 14
    • 23244445172 scopus 로고    scopus 로고
    • Development of a minimal cell-free translation system for the synthesis of presecretory and integral membrane proteins
    • Kuruma Y., Nishiyama K., Shimizu Y., Muller M., and Ueda T. Development of a minimal cell-free translation system for the synthesis of presecretory and integral membrane proteins. Biotechnol. Prog. 21 (2005) 1243-1251
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1243-1251
    • Kuruma, Y.1    Nishiyama, K.2    Shimizu, Y.3    Muller, M.4    Ueda, T.5
  • 16
    • 4344670572 scopus 로고    scopus 로고
    • Substrate replenishment extends protein synthesis with an in vitro translation system designed to mimic the cytoplasm
    • Jewett M.C., and Swartz J.R. Substrate replenishment extends protein synthesis with an in vitro translation system designed to mimic the cytoplasm. Biotechnol. Bioeng. 87 (2004) 465-472
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 465-472
    • Jewett, M.C.1    Swartz, J.R.2
  • 17
    • 33644482783 scopus 로고    scopus 로고
    • Stanford University, Stanford
    • Jewett M.C. Chemical Engineering (2004), Stanford University, Stanford 240
    • (2004) Chemical Engineering , pp. 240
    • Jewett, M.C.1
  • 18
    • 0033548545 scopus 로고    scopus 로고
    • Direct evidence that the proton motive force inhibits membrane translocation of positively charged residues within membrane proteins
    • Schuenemann T.A., Delgado-Nixon V.M., and Dalbey R.E. Direct evidence that the proton motive force inhibits membrane translocation of positively charged residues within membrane proteins. J. Biol. Chem. 274 (1999) 6855-6864
    • (1999) J. Biol. Chem. , vol.274 , pp. 6855-6864
    • Schuenemann, T.A.1    Delgado-Nixon, V.M.2    Dalbey, R.E.3
  • 19
    • 33845454189 scopus 로고    scopus 로고
    • Rapid expression of functional genomic libraries
    • Woodrow K., Airen I.O., and Swartz J.R. Rapid expression of functional genomic libraries. J. Proteome Res. 5 (2006) 3288-3300
    • (2006) J. Proteome Res. , vol.5 , pp. 3288-3300
    • Woodrow, K.1    Airen, I.O.2    Swartz, J.R.3
  • 21
    • 33646126496 scopus 로고    scopus 로고
    • Total amino acid stabilization during cell-free protein synthesis reactions
    • Calhoun K.A., and Swartz J.R. Total amino acid stabilization during cell-free protein synthesis reactions. J. Biotechnol. 123 (2006) 193-203
    • (2006) J. Biotechnol. , vol.123 , pp. 193-203
    • Calhoun, K.A.1    Swartz, J.R.2
  • 22
    • 1542720448 scopus 로고    scopus 로고
    • Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis
    • Jewett M.C., and Swartz J.R. Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol. Bioeng. 86 (2004) 19-26
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 19-26
    • Jewett, M.C.1    Swartz, J.R.2
  • 23
    • 0032575051 scopus 로고    scopus 로고
    • A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants
    • Hoang T.T., Karkhoff-Schweizer R.R., Kutchma A.J., and Schweizer H.P. A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants. Gene 212 (1998) 77-86
    • (1998) Gene , vol.212 , pp. 77-86
    • Hoang, T.T.1    Karkhoff-Schweizer, R.R.2    Kutchma, A.J.3    Schweizer, H.P.4
  • 24
    • 0037406142 scopus 로고    scopus 로고
    • The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome
    • Gu S.Q., Peske F., Wieden H.J., Rodnina M.V., and Wintermeyer W. The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome. RNA 9 (2003) 566-573
    • (2003) RNA , vol.9 , pp. 566-573
    • Gu, S.Q.1    Peske, F.2    Wieden, H.J.3    Rodnina, M.V.4    Wintermeyer, W.5
  • 25
    • 0034723143 scopus 로고    scopus 로고
    • Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP
    • Jagath J.R., Rodnina M.V., and Wintermeyer W. Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP. J. Mol. Biol. 295 (2000) 745-753
    • (2000) J. Mol. Biol. , vol.295 , pp. 745-753
    • Jagath, J.R.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 26
    • 3242691402 scopus 로고    scopus 로고
    • High-density, defined media culture for the production of Escherichia coli cell extracts
    • Saha B. (Ed), American Chemical Society, Washington, DC
    • Zawada J., Richter B., Huang E., Lodes E., Shah A., and Swartz J.R. High-density, defined media culture for the production of Escherichia coli cell extracts. In: Saha B. (Ed). Fermentation Biotechnology (2003), American Chemical Society, Washington, DC 142-156
    • (2003) Fermentation Biotechnology , pp. 142-156
    • Zawada, J.1    Richter, B.2    Huang, E.3    Lodes, E.4    Shah, A.5    Swartz, J.R.6
  • 27
    • 0015523228 scopus 로고
    • Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane
    • Osborn M.J., Gander J.E., Parisi E., and Carson J. Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. J. Biol. Chem. 247 (1972) 3962-3972
    • (1972) J. Biol. Chem. , vol.247 , pp. 3962-3972
    • Osborn, M.J.1    Gander, J.E.2    Parisi, E.3    Carson, J.4
  • 28
    • 0037829232 scopus 로고
    • In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coli
    • Muller M., and Blobel G. In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 7421-7425
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 7421-7425
    • Muller, M.1    Blobel, G.2
  • 29
    • 0015956843 scopus 로고
    • Proteins of the inner membrane of Escherichia coli: identification of succinate dehydrogenase by polyacrylamide gel electrophoresis with sdh amber mutants
    • Spencer M.E., and Guest J.R. Proteins of the inner membrane of Escherichia coli: identification of succinate dehydrogenase by polyacrylamide gel electrophoresis with sdh amber mutants. J. Bacteriol. 117 (1974) 947-953
    • (1974) J. Bacteriol. , vol.117 , pp. 947-953
    • Spencer, M.E.1    Guest, J.R.2
  • 30
    • 0023840230 scopus 로고
    • ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification
    • Grodberg J., and Dunn J.J. ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification. J. Bacteriol. 170 (1988) 1245-1253
    • (1988) J. Bacteriol. , vol.170 , pp. 1245-1253
    • Grodberg, J.1    Dunn, J.J.2
  • 31
    • 0442289581 scopus 로고    scopus 로고
    • Prokaryotic systems for in vitro expression
    • Weiner M., and Lu Q. (Eds), Eaton Publishing, Westborough, MA
    • Jewett M.C., Voloshin A., and Swartz J. Prokaryotic systems for in vitro expression. In: Weiner M., and Lu Q. (Eds). Gene Cloning and Expression Technologies (2002), Eaton Publishing, Westborough, MA 391-411
    • (2002) Gene Cloning and Expression Technologies , pp. 391-411
    • Jewett, M.C.1    Voloshin, A.2    Swartz, J.3
  • 32
    • 23244462601 scopus 로고    scopus 로고
    • Efficient and scalable method for scaling up cell free protein synthesis in batch mode
    • Voloshin A.M., and Swartz J.R. Efficient and scalable method for scaling up cell free protein synthesis in batch mode. Biotechnol. Bioeng. 91 (2005) 516-521
    • (2005) Biotechnol. Bioeng. , vol.91 , pp. 516-521
    • Voloshin, A.M.1    Swartz, J.R.2
  • 33
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E.G., and Dyer W.J. A rapid method of total lipid extraction and purification. Can. J. Biochem. Phys. 37 (1959) 911-917
    • (1959) Can. J. Biochem. Phys. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 34
    • 4244120872 scopus 로고
    • Microdetermination of phosphorus
    • Chen P.S., Toribara T.Y., and Warner H. Microdetermination of phosphorus. Anal. Chem. 28 (1956) 1756-1758
    • (1956) Anal. Chem. , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 36
    • 0030022717 scopus 로고    scopus 로고
    • Purification of the Tn10-specified tetracycline efflux antiporter TetA in a native state as a polyhistidine fusion protein
    • Aldema M.L., McMurry L.M., Walmsley A.R., and Levy S.B. Purification of the Tn10-specified tetracycline efflux antiporter TetA in a native state as a polyhistidine fusion protein. Mol. Microbiol. 19 (1996) 187-195
    • (1996) Mol. Microbiol. , vol.19 , pp. 187-195
    • Aldema, M.L.1    McMurry, L.M.2    Walmsley, A.R.3    Levy, S.B.4
  • 37
    • 0033983613 scopus 로고    scopus 로고
    • Permeation of tetracyclines through membranes of liposomes and Escherichia coli
    • Sigler A., Schubert P., Hillen W., and Niederweis M. Permeation of tetracyclines through membranes of liposomes and Escherichia coli. Eur. J. Biochem. 267 (2000) 527-534
    • (2000) Eur. J. Biochem. , vol.267 , pp. 527-534
    • Sigler, A.1    Schubert, P.2    Hillen, W.3    Niederweis, M.4
  • 38
    • 0345515642 scopus 로고
    • Active efflux of tetracycline encoded by four genetically different tetracycline resistance determinants in Escherichia coli
    • McMurry L., Petrucci Jr. R.E., and Levy S.B. Active efflux of tetracycline encoded by four genetically different tetracycline resistance determinants in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 3974-3977
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 3974-3977
    • McMurry, L.1    Petrucci Jr., R.E.2    Levy, S.B.3
  • 39
    • 0034602846 scopus 로고    scopus 로고
    • Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor
    • Beck K., Wu L.F., Brunner J., and Muller M. Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor. EMBO J. 19 (2000) 134-143
    • (2000) EMBO J. , vol.19 , pp. 134-143
    • Beck, K.1    Wu, L.F.2    Brunner, J.3    Muller, M.4
  • 40
    • 20044388542 scopus 로고    scopus 로고
    • FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon
    • Angelini S., Deitermann S., and Koch H.G. FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon. EMBO Rep. 6 (2005) 476-481
    • (2005) EMBO Rep. , vol.6 , pp. 476-481
    • Angelini, S.1    Deitermann, S.2    Koch, H.G.3
  • 41
    • 0034859711 scopus 로고    scopus 로고
    • YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids
    • Beck K., Eisner G., Trescher D., Dalbey R.E., Brunner J., and Muller M. YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids. EMBO Rep. 2 (2001) 709-714
    • (2001) EMBO Rep. , vol.2 , pp. 709-714
    • Beck, K.1    Eisner, G.2    Trescher, D.3    Dalbey, R.E.4    Brunner, J.5    Muller, M.6
  • 42
    • 0025318470 scopus 로고
    • Regulated high-level expression of the mannitol permease of the phosphoenolpyruvate-dependent sugar phosphotransferase system in Escherichia coli
    • van Weeghel R.P., Keck W., and Robillard G.T. Regulated high-level expression of the mannitol permease of the phosphoenolpyruvate-dependent sugar phosphotransferase system in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 2613-2617
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 2613-2617
    • van Weeghel, R.P.1    Keck, W.2    Robillard, G.T.3
  • 43
    • 0021034385 scopus 로고
    • Mannitol-specific enzyme II of the bacterial phosphotransferase system. I. Properties of the purified permease
    • Jacobson G.R., Lee C.A., Leonard J.E., and Saier Jr. M.H. Mannitol-specific enzyme II of the bacterial phosphotransferase system. I. Properties of the purified permease. J. Biol. Chem. 258 (1983) 10748-10756
    • (1983) J. Biol. Chem. , vol.258 , pp. 10748-10756
    • Jacobson, G.R.1    Lee, C.A.2    Leonard, J.E.3    Saier Jr., M.H.4
  • 44
    • 0026052185 scopus 로고
    • Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions
    • Sugiyama J.E., Mahmoodian S., and Jacobson G.R. Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 9603-9607
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 9603-9607
    • Sugiyama, J.E.1    Mahmoodian, S.2    Jacobson, G.R.3
  • 45
    • 0026464916 scopus 로고
    • Membrane insertion of the mannitol permease of Escherichia coli occurs under conditions of impaired SecA function
    • Werner P.K., Saier M.H., and Muller M. Membrane insertion of the mannitol permease of Escherichia coli occurs under conditions of impaired SecA function. J. Biol. Chem. 267 (1992) 24523-24532
    • (1992) J. Biol. Chem. , vol.267 , pp. 24523-24532
    • Werner, P.K.1    Saier, M.H.2    Muller, M.3
  • 46
    • 0032816265 scopus 로고    scopus 로고
    • In vitro studies with purified components reveal signal recognition particle (SRP) and SecA/SecB as constituents of two independent protein-targeting pathways of Escherichia coli
    • Koch H.G., Hengelage T., Neumann-Haefelin C., MacFarlane J., Hoffschulte H.K., Schimz K.L., Mechler B., and Muller M. In vitro studies with purified components reveal signal recognition particle (SRP) and SecA/SecB as constituents of two independent protein-targeting pathways of Escherichia coli. Mol. Biol. Cell 10 (1999) 2163-2173
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2163-2173
    • Koch, H.G.1    Hengelage, T.2    Neumann-Haefelin, C.3    MacFarlane, J.4    Hoffschulte, H.K.5    Schimz, K.L.6    Mechler, B.7    Muller, M.8
  • 48
    • 23244446620 scopus 로고    scopus 로고
    • Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis
    • Underwood K.A., Swartz J.R., and Puglisi J.D. Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis. Biotechnol. Bioeng. 91 (2005) 425-435
    • (2005) Biotechnol. Bioeng. , vol.91 , pp. 425-435
    • Underwood, K.A.1    Swartz, J.R.2    Puglisi, J.D.3
  • 50
    • 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., and Walker J.E. 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 (1996) 289-298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 51
    • 0034613080 scopus 로고    scopus 로고
    • Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over-production of the b subunit of F1F0 ATP synthase
    • Arechaga I., Miroux B., Karrasch S., Huijbregts R., de Kruijff B., Runswick M.J., and Walker J.E. Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over-production of the b subunit of F1F0 ATP synthase. FEBS Lett. 482 (2000) 215-219
    • (2000) FEBS Lett. , vol.482 , pp. 215-219
    • Arechaga, I.1    Miroux, B.2    Karrasch, S.3    Huijbregts, R.4    de Kruijff, B.5    Runswick, M.J.6    Walker, J.E.7
  • 52
    • 0017684842 scopus 로고
    • Mutants of Escherichia coli defective in membrane phospholipid synthesis-effects of cessation and reinitiation of phospholipid synthesis on macromolecular-synthesis and phospholipid turnover
    • McIntyre T.M., Chamberlain B.K., Webster R.E., and Bell R.M. Mutants of Escherichia coli defective in membrane phospholipid synthesis-effects of cessation and reinitiation of phospholipid synthesis on macromolecular-synthesis and phospholipid turnover. J. Biol. Chem. 252 (1977) 4487-4493
    • (1977) J. Biol. Chem. , vol.252 , pp. 4487-4493
    • McIntyre, T.M.1    Chamberlain, B.K.2    Webster, R.E.3    Bell, R.M.4
  • 53
    • 28244458078 scopus 로고    scopus 로고
    • Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system
    • Klammt C., Schwarz D., Fendler K., Haase W., Dotsch V., and Bernhard F. Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system. FEBS J. 272 (2005) 6024-6038
    • (2005) FEBS J. , vol.272 , pp. 6024-6038
    • Klammt, C.1    Schwarz, D.2    Fendler, K.3    Haase, W.4    Dotsch, V.5    Bernhard, F.6
  • 54
    • 0037102542 scopus 로고    scopus 로고
    • Mutational analysis of tetracycline resistance protein transmembrane segment insertion
    • Lewis G.S., Jewell J.E., Phang T., and Miller K.W. Mutational analysis of tetracycline resistance protein transmembrane segment insertion. Arch. Biochem. Biophys. 404 (2002) 317-325
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 317-325
    • Lewis, G.S.1    Jewell, J.E.2    Phang, T.3    Miller, K.W.4
  • 57
    • 4944248085 scopus 로고    scopus 로고
    • F1F0 ATP synthase subunit c is targeted by the SRP to YidC in the E. coli inner membrane
    • van Bloois E., Haan G.J., de Gier J.W., Oudega B., and Luirink J. F1F0 ATP synthase subunit c is targeted by the SRP to YidC in the E. coli inner membrane. FEBS Lett. 576 (2004) 97-100
    • (2004) FEBS Lett. , vol.576 , pp. 97-100
    • van Bloois, E.1    Haan, G.J.2    de Gier, J.W.3    Oudega, B.4    Luirink, J.5
  • 58
    • 0141789788 scopus 로고    scopus 로고
    • A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase
    • Hatzixanthis K., Palmer T., and Sargent F. A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase. Mol. Microbiol. 49 (2003) 1377-1390
    • (2003) Mol. Microbiol. , vol.49 , pp. 1377-1390
    • Hatzixanthis, K.1    Palmer, T.2    Sargent, F.3
  • 59
    • 28244452583 scopus 로고    scopus 로고
    • A dual function for SecA in the assembly of single spanning membrane proteins in Escherichia coli
    • Deitermann S., Sprie G.S., and Koch H.G. A dual function for SecA in the assembly of single spanning membrane proteins in Escherichia coli. J. Biol. Chem. 280 (2005) 39077-39085
    • (2005) J. Biol. Chem. , vol.280 , pp. 39077-39085
    • Deitermann, S.1    Sprie, G.S.2    Koch, H.G.3
  • 60
    • 0038580973 scopus 로고    scopus 로고
    • Mutational and sequence analysis of transmembrane segment 6 orientation in TetA proteins
    • Lewis G.S., Jewell J.E., Phang T., and Miller K.W. Mutational and sequence analysis of transmembrane segment 6 orientation in TetA proteins. Biochem. Biophys. Res. Commun. 305 (2003) 1067-1072
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 1067-1072
    • Lewis, G.S.1    Jewell, J.E.2    Phang, T.3    Miller, K.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.