메뉴 건너뛰기




Volumn 258, Issue , 2017, Pages 101-109

Beyond amino acids: Use of the Corynebacterium glutamicum cell factory for the secretion of heterologous proteins

Author keywords

Corynebacterium glutamicum; Expression platform organism; Heterologous protein secretion; Sec system; Signal peptide; Twin arginine translocation

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; CELL MEMBRANES; PHYSIOLOGY;

EID: 85014240106     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2017.02.023     Document Type: Article
Times cited : (44)

References (71)
  • 1
    • 0036135189 scopus 로고    scopus 로고
    • Expression of the genes coding for the xylanase Xys1 and the cellulase Cel1 from the straw-decomposing Streptomyces halstedii JM8 cloned into the amino-acid producer Brevibacterium lactofermentum ATCC13869
    • Adham, S.A.I., Honrubia, P., Diaz, M., Fernadez-Abalos, J., Santamaria, R.I., Gil, J.A., Expression of the genes coding for the xylanase Xys1 and the cellulase Cel1 from the straw-decomposing Streptomyces halstedii JM8 cloned into the amino-acid producer Brevibacterium lactofermentum ATCC13869. Arch. Microbiol. 177 (2001), 91–97.
    • (2001) Arch. Microbiol. , vol.177 , pp. 91-97
    • Adham, S.A.I.1    Honrubia, P.2    Diaz, M.3    Fernadez-Abalos, J.4    Santamaria, R.I.5    Gil, J.A.6
  • 2
    • 10744228022 scopus 로고    scopus 로고
    • Differential interaction between a twin-arginine signal peptide and its translocase in Escherichia coli
    • Alami, M., Lüke, I., Deitermann, S., Eisner, G., Koch, H.-G., Brunner, J., Müller, M., Differential interaction between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol. Cell 12 (2003), 937–946.
    • (2003) Mol. Cell , vol.12 , pp. 937-946
    • Alami, M.1    Lüke, I.2    Deitermann, S.3    Eisner, G.4    Koch, H.-G.5    Brunner, J.6    Müller, M.7
  • 3
    • 84876976144 scopus 로고    scopus 로고
    • Development of a secretion system for the production of heterologous proteins in Corynebacterium glutamicum using the Porin B signal peptide
    • An, S.J., Yim, S.S., Jeong, K.J., Development of a secretion system for the production of heterologous proteins in Corynebacterium glutamicum using the Porin B signal peptide. Protein Expr. Purif. 89 (2013), 251–257.
    • (2013) Protein Expr. Purif. , vol.89 , pp. 251-257
    • An, S.J.1    Yim, S.S.2    Jeong, K.J.3
  • 4
    • 0041429588 scopus 로고    scopus 로고
    • Mycomembrane and S-layer: two important structures of Corynebacterium glutamicum cell envelope with promising biotechnology applications
    • Bayan, N., Houssin, C., Chami, M., Leblon, G., Mycomembrane and S-layer: two important structures of Corynebacterium glutamicum cell envelope with promising biotechnology applications. J. Biotechnol. 104 (2003), 55–67.
    • (2003) J. Biotechnol. , vol.104 , pp. 55-67
    • Bayan, N.1    Houssin, C.2    Chami, M.3    Leblon, G.4
  • 5
  • 6
    • 84864801619 scopus 로고    scopus 로고
    • Bio-based production of chemicals, materials and fuels −Corynebacterium glutamicum as versatile cell factory
    • Becker, J., Wittmann, C., Bio-based production of chemicals, materials and fuels −Corynebacterium glutamicum as versatile cell factory. Curr. Opin. Biotechnol. 23 (2012), 631–640.
    • (2012) Curr. Opin. Biotechnol. , vol.23 , pp. 631-640
    • Becker, J.1    Wittmann, C.2
  • 7
    • 85028969831 scopus 로고    scopus 로고
    • Corynebacterium glutamicum strain with enhanced secretion activity
    • United States Patent US 6, 982, 162, B2.
    • Berens, S., Kalinowski, J., Pühler, A., 2006. Corynebacterium glutamicum strain with enhanced secretion activity. United States Patent US 6, 982, 162, B2.
    • (2006)
    • Berens, S.1    Kalinowski, J.2    Pühler, A.3
  • 9
    • 33748101074 scopus 로고    scopus 로고
    • Systematic screening of all signal peptides from Bacillus subtilis: a powerful strategy in optimizing heterologous protein secretion in Gram-positive bacteria
    • Brockmeier, U., Caspers, M., Freudl, R., Jockwer, A., Noll, T., Eggert, T., Systematic screening of all signal peptides from Bacillus subtilis: a powerful strategy in optimizing heterologous protein secretion in Gram-positive bacteria. J. Mol. Biol. 362 (2006), 393–402.
    • (2006) J. Mol. Biol. , vol.362 , pp. 393-402
    • Brockmeier, U.1    Caspers, M.2    Freudl, R.3    Jockwer, A.4    Noll, T.5    Eggert, T.6
  • 10
    • 0026486248 scopus 로고
    • Expression of Streptomyces genes encoding extracellular enzymes in Brevibacterium lactofermentum: secretion proceeds by removal of the same leader peptide as in Streptomyces lividans
    • Cadenas, R.F., Gil, J.A., Martin, J.F., Expression of Streptomyces genes encoding extracellular enzymes in Brevibacterium lactofermentum: secretion proceeds by removal of the same leader peptide as in Streptomyces lividans. Appl. Microbiol. Biotechnol. 38 (1992), 362–369.
    • (1992) Appl. Microbiol. Biotechnol. , vol.38 , pp. 362-369
    • Cadenas, R.F.1    Gil, J.A.2    Martin, J.F.3
  • 11
    • 36549015182 scopus 로고    scopus 로고
    • Production of humanized glycoproteins in bacteria and yeasts
    • Chiba, Y., Jigami, Y., Production of humanized glycoproteins in bacteria and yeasts. Curr. Opin. Chem. Biol. 11 (2007), 670–676.
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 670-676
    • Chiba, Y.1    Jigami, Y.2
  • 12
    • 0038219967 scopus 로고    scopus 로고
    • Production of native-type Streptoverticillium mobaraense transglutaminase in Corynebacterium glutamicum
    • Date, M., Yokoyama K.-i. Umezawa, Y., Matsui, H., Kikuchi, Y., Production of native-type Streptoverticillium mobaraense transglutaminase in Corynebacterium glutamicum. Appl. Environ. Microbiol. 69 (2003), 3011–3014.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 3011-3014
    • Date, M.1    Yokoyama K.-i. Umezawa, Y.2    Matsui, H.3    Kikuchi, Y.4
  • 13
    • 2442516249 scopus 로고    scopus 로고
    • High level expression of Streptomyces mobaraensis transglutaminase in Corynebacterium glutamicum using a chimeric pro-region from Streptomyces cinnamoneus transglutaminase
    • Date, M., Yokoyama K.-i. Umezawa, Y., Matsui, H., Kikuchi, Y., High level expression of Streptomyces mobaraensis transglutaminase in Corynebacterium glutamicum using a chimeric pro-region from Streptomyces cinnamoneus transglutaminase. J. Biotechnol. 110 (2004), 219–226.
    • (2004) J. Biotechnol. , vol.110 , pp. 219-226
    • Date, M.1    Yokoyama K.-i. Umezawa, Y.2    Matsui, H.3    Kikuchi, Y.4
  • 14
    • 33645229632 scopus 로고    scopus 로고
    • Secretion of human epidermal growth factor by Corynebacterium glutamicum
    • Date, M., Itaya, H., Matsui, H., Kikuchi, Y., Secretion of human epidermal growth factor by Corynebacterium glutamicum. Lett. Appl. Microbiol. 42 (2006), 66–70.
    • (2006) Lett. Appl. Microbiol. , vol.42 , pp. 66-70
    • Date, M.1    Itaya, H.2    Matsui, H.3    Kikuchi, Y.4
  • 18
    • 84967185263 scopus 로고    scopus 로고
    • Framework for Kriging-based iterative experimental analysis and design: optimization of secretory protein production in Corynebacterium glutamicum
    • Freier, L., Hemmerich, J., Schöler, K., Wiechert, W., Oldiges, M., von Lieres, E., Framework for Kriging-based iterative experimental analysis and design: optimization of secretory protein production in Corynebacterium glutamicum. Eng. Life Sci. 16 (2016), 538–549.
    • (2016) Eng. Life Sci. , vol.16 , pp. 538-549
    • Freier, L.1    Hemmerich, J.2    Schöler, K.3    Wiechert, W.4    Oldiges, M.5    von Lieres, E.6
  • 19
    • 84879882380 scopus 로고    scopus 로고
    • Leaving home aińt easy – protein export systems in Gram-positive bacteria
    • Freudl, R., Leaving home aińt easy – protein export systems in Gram-positive bacteria. Res. Microbiol. 164 (2013), 664–674.
    • (2013) Res. Microbiol. , vol.164 , pp. 664-674
    • Freudl, R.1
  • 20
    • 85029005935 scopus 로고    scopus 로고
    • Corynebacterium glutamicum as a platform organism for the secretory production of heterologous proteins
    • A. Burkovski Caister Academic Press Norfolk UK
    • Freudl, R., Corynebacterium glutamicum as a platform organism for the secretory production of heterologous proteins. Burkovski, A., (eds.) Corynebacterium glutamicum: From Systems Biology to Biotechnological Application, 2015, Caister Academic Press Norfolk, UK, 161–177.
    • (2015) Corynebacterium glutamicum: From Systems Biology to Biotechnological Application , pp. 161-177
    • Freudl, R.1
  • 21
    • 39049125071 scopus 로고    scopus 로고
    • Bacillus protein secretion: an unfolding story
    • Harwood, C.R., Cranenburgh, R., Bacillus protein secretion: an unfolding story. Trends Microbiol. 16 (2008), 73–79.
    • (2008) Trends Microbiol. , vol.16 , pp. 73-79
    • Harwood, C.R.1    Cranenburgh, R.2
  • 22
    • 85002639893 scopus 로고    scopus 로고
    • Use of a Sec signal peptide library from Bacillus subtilis for the optimization of cutinase secretion in Corynebacterium glutamicum
    • Hemmerich, J., Rohe, P., Kleine, B., Jurischka, S., Wiechert, W., Freudl, R., Oldiges, M., Use of a Sec signal peptide library from Bacillus subtilis for the optimization of cutinase secretion in Corynebacterium glutamicum. Microb. Cell Fact., 15, 2016, 208.
    • (2016) Microb. Cell Fact. , vol.15 , pp. 208
    • Hemmerich, J.1    Rohe, P.2    Kleine, B.3    Jurischka, S.4    Wiechert, W.5    Freudl, R.6    Oldiges, M.7
  • 23
    • 0032947597 scopus 로고    scopus 로고
    • Temporal expression of the Bacillus subtilis secA gene, encoding a central component of the preprotein translocase
    • Herbort, M., Klein, M., Manting, E.H., Driessen, A.J.M., Freudl, R., Temporal expression of the Bacillus subtilis secA gene, encoding a central component of the preprotein translocase. J. Bacteriol. 181 (1999), 493–500.
    • (1999) J. Bacteriol. , vol.181 , pp. 493-500
    • Herbort, M.1    Klein, M.2    Manting, E.H.3    Driessen, A.J.M.4    Freudl, R.5
  • 24
    • 41649116701 scopus 로고    scopus 로고
    • Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure
    • Hoffmann, C., Leis, A., Niederweis, M., Plitzko, J.M., Engelhardt, H., Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure. Proc. Natl. Acad. Sci. U. S. A. 105 (2008), 3963–3967.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 3963-3967
    • Hoffmann, C.1    Leis, A.2    Niederweis, M.3    Plitzko, J.M.4    Engelhardt, H.5
  • 25
    • 0035118223 scopus 로고    scopus 로고
    • Constitutive expression of Escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth
    • Jack, R.L., Sargent, F., Berks, B.C., Sawers, G., Palmer, T., Constitutive expression of Escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth. J. Bacteriol. 183 (2001), 1801–1804.
    • (2001) J. Bacteriol. , vol.183 , pp. 1801-1804
    • Jack, R.L.1    Sargent, F.2    Berks, B.C.3    Sawers, G.4    Palmer, T.5
  • 26
    • 0037229834 scopus 로고    scopus 로고
    • Secretion of active-form Streptoverticillum mobaraense transglutaminase by Corynebacterium glutamicum: processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus
    • Kikuchi, Y., Date, M., Yokoyama -i. Umezawa, K.Y., Matsui, H., Secretion of active-form Streptoverticillum mobaraense transglutaminase by Corynebacterium glutamicum: processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus. Appl. Environ. Microbiol. 69 (2003), 358–366.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 358-366
    • Kikuchi, Y.1    Date, M.2    Yokoyama -i. Umezawa, K.Y.3    Matsui, H.4
  • 27
    • 33750973650 scopus 로고    scopus 로고
    • Functional analysis of the twin-arginine translocation pathway in Corynebacterium glutamicum ATCC 13869
    • Kikuchi, Y., Date, M., Itaya, H., Matsui, K., Wu, L.-F., Functional analysis of the twin-arginine translocation pathway in Corynebacterium glutamicum ATCC 13869. Appl. Environ. Microbiol. 72 (2006), 7183–7192.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 7183-7192
    • Kikuchi, Y.1    Date, M.2    Itaya, H.3    Matsui, K.4    Wu, L.-F.5
  • 28
    • 38349189461 scopus 로고    scopus 로고
    • Production of Chryseobacterium proteolyticum protein-glutaminase using the twin-arginine translocation pathway in Corynebacterium glutamicum
    • Kikuchi, Y., Itaya, H., Date, M., Matsui, K., Wu, L.-F., Production of Chryseobacterium proteolyticum protein-glutaminase using the twin-arginine translocation pathway in Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 78 (2008), 67–74.
    • (2008) Appl. Microbiol. Biotechnol. , vol.78 , pp. 67-74
    • Kikuchi, Y.1    Itaya, H.2    Date, M.3    Matsui, K.4    Wu, L.-F.5
  • 29
    • 59649085581 scopus 로고    scopus 로고
    • TatABC overexpression improves Corynebacterium glutamicum Tat-dependent protein secretion
    • Kikuchi, Y., Itaya, H., Date, M., Matsui, K., Wu, L.-F., TatABC overexpression improves Corynebacterium glutamicum Tat-dependent protein secretion. Appl. Environ. Microbiol. 75 (2009), 603–607.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 603-607
    • Kikuchi, Y.1    Itaya, H.2    Date, M.3    Matsui, K.4    Wu, L.-F.5
  • 30
    • 71449087260 scopus 로고    scopus 로고
    • Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB
    • Lüke, I., Hanford, J.I., Palmer, T., Sargent, F., Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB. Arch. Microbiol. 191 (2009), 919–925.
    • (2009) Arch. Microbiol. , vol.191 , pp. 919-925
    • Lüke, I.1    Hanford, J.I.2    Palmer, T.3    Sargent, F.4
  • 31
    • 33846837274 scopus 로고    scopus 로고
    • The alternative sigma factor SigB of Corynebacterium glutamicum modulates global gene expression during transition from exponential growth to stationary phase
    • Larisch, C., Nakunst, D., Hüser, A.T., Tauch, A., Kalinowski, J., The alternative sigma factor SigB of Corynebacterium glutamicum modulates global gene expression during transition from exponential growth to stationary phase. BMC Genomics, 8, 2007, 4.
    • (2007) BMC Genomics , vol.8 , pp. 4
    • Larisch, C.1    Nakunst, D.2    Hüser, A.T.3    Tauch, A.4    Kalinowski, J.5
  • 32
    • 84862746985 scopus 로고    scopus 로고
    • Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli
    • Lausberg, F., Fleckenstein, S., Kreutzenbeck, P., Fröbel, J., Rose, P., Müller, M., Freudl, R., Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli. PLoS ONE, 7, 2012, e39867.
    • (2012) PLoS ONE , vol.7 , pp. e39867
    • Lausberg, F.1    Fleckenstein, S.2    Kreutzenbeck, P.3    Fröbel, J.4    Rose, P.5    Müller, M.6    Freudl, R.7
  • 33
    • 4544240395 scopus 로고    scopus 로고
    • Bottlenecks in the expression and secretion of heterologous proteins in Bacillus subtilis
    • Li, W., Zhou, X., Lu, P., Bottlenecks in the expression and secretion of heterologous proteins in Bacillus subtilis. Res. Microbiol. 155 (2004), 605–610.
    • (2004) Res. Microbiol. , vol.155 , pp. 605-610
    • Li, W.1    Zhou, X.2    Lu, P.3
  • 34
    • 0026553915 scopus 로고
    • Expression, secretion, and processing of staphylococcal nuclease by Corynebacterium glutamicum
    • Liebl, W., Sinskey, A.J., Schleifer, K.-H., Expression, secretion, and processing of staphylococcal nuclease by Corynebacterium glutamicum. J. Bacteriol. 174 (1992), 1854–1861.
    • (1992) J. Bacteriol. , vol.174 , pp. 1854-1861
    • Liebl, W.1    Sinskey, A.J.2    Schleifer, K.-H.3
  • 35
    • 84905120092 scopus 로고    scopus 로고
    • A novel approach for improving the yield of Bacillus subtilis transglutaminase in heterologous strains
    • Liu, Y., Lin, S., Zhang, X., Liu, X., Wang, J., Lu, F., A novel approach for improving the yield of Bacillus subtilis transglutaminase in heterologous strains. J. Ind. Microbiol. Biotechnol. 41 (2014), 1227–1235.
    • (2014) J. Ind. Microbiol. Biotechnol. , vol.41 , pp. 1227-1235
    • Liu, Y.1    Lin, S.2    Zhang, X.3    Liu, X.4    Wang, J.5    Lu, F.6
  • 36
    • 84906828928 scopus 로고    scopus 로고
    • High-level expression of the Streptomyces mobaraense CICC 11018 transglutaminase in Corynebacterium glutamicum ATCC 13032
    • Liu, Y.H., Lin, S., Liu, K., Liu, X.G., Zhang, X.Q., Wang, H.B., Lu, F.P., High-level expression of the Streptomyces mobaraense CICC 11018 transglutaminase in Corynebacterium glutamicum ATCC 13032. Appl. Biochem. Microbiol. 50 (2014), 456–462.
    • (2014) Appl. Biochem. Microbiol. , vol.50 , pp. 456-462
    • Liu, Y.H.1    Lin, S.2    Liu, K.3    Liu, X.G.4    Zhang, X.Q.5    Wang, H.B.6    Lu, F.P.7
  • 38
    • 0032476656 scopus 로고    scopus 로고
    • A role for trigger factor and an Rgg-like regulator in the transcription: secretion and processing of the cysteine proteinase of Streptococcus pyogenes
    • Lyon, W.R., Gibson, C.M., Caparon, M.G., A role for trigger factor and an Rgg-like regulator in the transcription: secretion and processing of the cysteine proteinase of Streptococcus pyogenes. EMBO J. 17 (1998), 6263–6275.
    • (1998) EMBO J. , vol.17 , pp. 6263-6275
    • Lyon, W.R.1    Gibson, C.M.2    Caparon, M.G.3
  • 39
    • 33744819460 scopus 로고    scopus 로고
    • The Corynebacterium glutamicum gene pmt encoding a glycosyltransferase related to eukaryotic protein-O-mannosyltransferases is essential for glycosylation of the resuscitation promoting factor (Rpf2) and other secreted proteins
    • Mahne, M., Tauch, A., Pühler, A., Kalinowski, J., The Corynebacterium glutamicum gene pmt encoding a glycosyltransferase related to eukaryotic protein-O-mannosyltransferases is essential for glycosylation of the resuscitation promoting factor (Rpf2) and other secreted proteins. FEMS Microbiol. Lett. 259 (2006), 226–233.
    • (2006) FEMS Microbiol. Lett. , vol.259 , pp. 226-233
    • Mahne, M.1    Tauch, A.2    Pühler, A.3    Kalinowski, J.4
  • 42
    • 34548019942 scopus 로고    scopus 로고
    • Comparative analysis of twin-arginine (Tat)-dependent protein secretion of a heterologous model protein (GFP) in three different Gram-positive bacteria
    • Meissner, D., Vollstedt, A., van Dijl, J.M., Freudl, R., Comparative analysis of twin-arginine (Tat)-dependent protein secretion of a heterologous model protein (GFP) in three different Gram-positive bacteria. Appl. Microbiol. Biotechnol. 76 (2007), 633–642.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 633-642
    • Meissner, D.1    Vollstedt, A.2    van Dijl, J.M.3    Freudl, R.4
  • 44
    • 84927130277 scopus 로고    scopus 로고
    • A TatABC-type Tat translocase is required for unimpaired aerobic growth of Corynebacterium glutamicum ATCC13023
    • Oertel, D., Schmitz, S., Freudl, R., A TatABC-type Tat translocase is required for unimpaired aerobic growth of Corynebacterium glutamicum ATCC13023. PLoS ONE, 10, 2015, e0123413.
    • (2015) PLoS ONE , vol.10 , pp. e0123413
    • Oertel, D.1    Schmitz, S.2    Freudl, R.3
  • 45
    • 84862501228 scopus 로고    scopus 로고
    • The twin-arginine translocation (Tat) protein export pathway
    • Palmer, T., Berks, B.C., The twin-arginine translocation (Tat) protein export pathway. Nat. Rev. Microbiol. 10 (2012), 483–496.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 483-496
    • Palmer, T.1    Berks, B.C.2
  • 46
    • 0023551810 scopus 로고
    • The expression of Cellulomonas fimi cellulase genes in Brevibacterium lactofermentum
    • Paradis, F.W., Warren, R.A.J., Kilburn, D.G., Miller, R.C. Jr., The expression of Cellulomonas fimi cellulase genes in Brevibacterium lactofermentum. Gene 61 (1987), 199–206.
    • (1987) Gene , vol.61 , pp. 199-206
    • Paradis, F.W.1    Warren, R.A.J.2    Kilburn, D.G.3    Miller, R.C.4
  • 47
    • 0030634338 scopus 로고    scopus 로고
    • Merits of secretion of heterologous proteins from industrial microorganisms
    • Quax, W.J., Merits of secretion of heterologous proteins from industrial microorganisms. Folia Microbiol. 42 (1997), 99–103.
    • (1997) Folia Microbiol. , vol.42 , pp. 99-103
    • Quax, W.J.1
  • 49
    • 84868259526 scopus 로고    scopus 로고
    • An automated workflow for enhancing microbial bioprocess optimization on a novel microbioreactor platform
    • Rohe, P., Venkanna, D., Kleine, B., Freudl, R., Oldiges, M., An automated workflow for enhancing microbial bioprocess optimization on a novel microbioreactor platform. Microb. Cell Fact., 11, 2012, 144.
    • (2012) Microb. Cell Fact. , vol.11 , pp. 144
    • Rohe, P.1    Venkanna, D.2    Kleine, B.3    Freudl, R.4    Oldiges, M.5
  • 50
    • 34548206622 scopus 로고    scopus 로고
    • Interactions that drive Sec-dependent bacterial protein transport
    • Rusch, S.L., Kendall, D.A., Interactions that drive Sec-dependent bacterial protein transport. Biochemistry 46 (2007), 9665–9673.
    • (2007) Biochemistry , vol.46 , pp. 9665-9673
    • Rusch, S.L.1    Kendall, D.A.2
  • 51
    • 0030658935 scopus 로고    scopus 로고
    • Heterologous expression of the Mycobacterium tuberculosis gene encoding antigen 85A in Corynebacterium glutamicum
    • Salim, K., Haedens, V., Content, J., Leblon, G., Huygen, K., Heterologous expression of the Mycobacterium tuberculosis gene encoding antigen 85A in Corynebacterium glutamicum. Appl. Environ. Microbiol. 63 (1997), 4392–4400.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4392-4400
    • Salim, K.1    Haedens, V.2    Content, J.3    Leblon, G.4    Huygen, K.5
  • 52
    • 79953752538 scopus 로고    scopus 로고
    • Molecular mechanism of co-translational protein targeting by the signal recognition particle
    • Saraogi, I., Shan, S.-o., Molecular mechanism of co-translational protein targeting by the signal recognition particle. Traffic 12 (2011), 535–542.
    • (2011) Traffic , vol.12 , pp. 535-542
    • Saraogi, I.1    Shan, S.-O.2
  • 53
    • 1642473932 scopus 로고    scopus 로고
    • The importance of the Tat-dependent protein secretion pathway in Streptomyces as revealed by phenotypic changes in tat deletion mutants and genome analysis
    • Schaerlaekens, K., Van Mellaert, L., Lammertyn, E., Geukens, N., Anné, J., The importance of the Tat-dependent protein secretion pathway in Streptomyces as revealed by phenotypic changes in tat deletion mutants and genome analysis. Microbiology (UK) 150 (2004), 21–31.
    • (2004) Microbiology (UK) , vol.150 , pp. 21-31
    • Schaerlaekens, K.1    Van Mellaert, L.2    Lammertyn, E.3    Geukens, N.4    Anné, J.5
  • 54
    • 84873964140 scopus 로고    scopus 로고
    • Secretory production of an FAD cofactor-containing cytosolic enzyme (sorbitol-xylitol oxidase from Streptomyces coelicolor) using the twin-arginine translocation (Tat) pathway of Corynebacterium glutamicum
    • Scheele, S., Oertel, D., Bongaerts, J., Evers, S., Hellmuth, H., Maurer, K.-H., Bott, M., Freudl, R., Secretory production of an FAD cofactor-containing cytosolic enzyme (sorbitol-xylitol oxidase from Streptomyces coelicolor) using the twin-arginine translocation (Tat) pathway of Corynebacterium glutamicum. Microb. Biotechnol. 6 (2013), 202–206.
    • (2013) Microb. Biotechnol. , vol.6 , pp. 202-206
    • Scheele, S.1    Oertel, D.2    Bongaerts, J.3    Evers, S.4    Hellmuth, H.5    Maurer, K.-H.6    Bott, M.7    Freudl, R.8
  • 55
    • 0022628563 scopus 로고
    • Protoplast transformation in coryneform bacteria and introduction of an alpha-amylase gene from Bacillus amyloliquefaciens into Brevibacterium lactofermentum
    • Smith, M.D., Flickinger, J.L., Lineberger, D.W., Schmidt, B., Protoplast transformation in coryneform bacteria and introduction of an alpha-amylase gene from Bacillus amyloliquefaciens into Brevibacterium lactofermentum. Appl. Environ. Microbiol. 51 (1986), 634–639.
    • (1986) Appl. Environ. Microbiol. , vol.51 , pp. 634-639
    • Smith, M.D.1    Flickinger, J.L.2    Lineberger, D.W.3    Schmidt, B.4
  • 56
    • 36248965184 scopus 로고    scopus 로고
    • Direct production of L-lysine from raw corn starch by Corynebacterium glutamicum secreting Streptococcus bovis α-amylase using cspB promoter and signal sequence
    • Tateno, H., Fukuda, H., Kondo, A., Direct production of L-lysine from raw corn starch by Corynebacterium glutamicum secreting Streptococcus bovis α-amylase using cspB promoter and signal sequence. Appl. Microbiol. Biotechnol. 77 (2007), 533–541.
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 533-541
    • Tateno, H.1    Fukuda, H.2    Kondo, A.3
  • 57
    • 79960739073 scopus 로고    scopus 로고
    • High yield secretion of heterologous proteins in Corynebacterium glutamicum using its own Tat-type signal sequence
    • Teramoto, H., Watanabe, K., Suzuki, N., Inui, M., Yukawa, H., High yield secretion of heterologous proteins in Corynebacterium glutamicum using its own Tat-type signal sequence. Appl. Microbiol. Biotechnol. 91 (2011), 677–687.
    • (2011) Appl. Microbiol. Biotechnol. , vol.91 , pp. 677-687
    • Teramoto, H.1    Watanabe, K.2    Suzuki, N.3    Inui, M.4    Yukawa, H.5
  • 61
    • 84876985466 scopus 로고    scopus 로고
    • Protein secretion systems of Corynebacterium glutamicum
    • H. Yukawa M. Inui Springer Verlag Berlin Heidelberg (Microbiology Monographs)
    • Vertès, A.A., Protein secretion systems of Corynebacterium glutamicum. Yukawa, H., Inui, M., (eds.) Corynebacterium glutamicum. Biology and Biotechnology, Vol. 23, 2013, Springer, Verlag Berlin Heidelberg, 351–389 (Microbiology Monographs).
    • (2013) Corynebacterium glutamicum. Biology and Biotechnology , vol.23 , pp. 351-389
    • Vertès, A.A.1
  • 62
    • 64049102180 scopus 로고    scopus 로고
    • Scanning the Corynebacterium glutamicum R genome for high-efficiency secretion signal sequences
    • Watanabe, K., Tsuchida, Y., Okibe, N., Teramoto, H., Suzuki, N., Inui, M., Yukawa, H., Scanning the Corynebacterium glutamicum R genome for high-efficiency secretion signal sequences. Microbiology (UK) 155 (2009), 741–750.
    • (2009) Microbiology (UK) , vol.155 , pp. 741-750
    • Watanabe, K.1    Tsuchida, Y.2    Okibe, N.3    Teramoto, H.4    Suzuki, N.5    Inui, M.6    Yukawa, H.7
  • 63
    • 84878011326 scopus 로고    scopus 로고
    • Influence of SigB inactivation on Corynebacterium glutamicum protein secretion
    • Watanabe, K., Teramoto, H., Suzuki, N., Inui, M., Yukawa, H., Influence of SigB inactivation on Corynebacterium glutamicum protein secretion. Appl. Microbiol. Biotechnol. 97 (2013), 4917–4926.
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 4917-4926
    • Watanabe, K.1    Teramoto, H.2    Suzuki, N.3    Inui, M.4    Yukawa, H.5
  • 65
    • 0032460995 scopus 로고    scopus 로고
    • Enhanced secretory production of a single-chain antibody fragment from Bacillus subtilis by coproduction of molecular chaperones
    • Wu, S.-C., Ye, R., Wu, X.-C., Ng, S.-C., Wong, S.-L., Enhanced secretory production of a single-chain antibody fragment from Bacillus subtilis by coproduction of molecular chaperones. J. Bacteriol. 180 (1998), 2830–2835.
    • (1998) J. Bacteriol. , vol.180 , pp. 2830-2835
    • Wu, S.-C.1    Ye, R.2    Wu, X.-C.3    Ng, S.-C.4    Wong, S.-L.5
  • 66
    • 84884532775 scopus 로고    scopus 로고
    • Isolation of fully synthetic promoters for high-level gene expression in Corynebacterium glutamicum
    • Yim, S.S., An, S.J., Kang, M., Lee, J., Jeong, K.J., Isolation of fully synthetic promoters for high-level gene expression in Corynebacterium glutamicum. Biotechnol. Bioeng. 110 (2013), 2959–2969.
    • (2013) Biotechnol. Bioeng. , vol.110 , pp. 2959-2969
    • Yim, S.S.1    An, S.J.2    Kang, M.3    Lee, J.4    Jeong, K.J.5
  • 67
    • 84891853096 scopus 로고    scopus 로고
    • High-level secretory production of recombinant single-chain variable fragment (scFv) in Corynebacterium glutamicum
    • Yim, S.S., An, S.J., Choi, J.W., Ryu, A.J., Jeong, K.J., High-level secretory production of recombinant single-chain variable fragment (scFv) in Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 98 (2014), 273–284.
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , pp. 273-284
    • Yim, S.S.1    An, S.J.2    Choi, J.W.3    Ryu, A.J.4    Jeong, K.J.5
  • 68
    • 84948119805 scopus 로고    scopus 로고
    • Development of a new platform for secretory production of recombinant proteins in Corynebacterium glutamicum
    • Yim, S.S., Choi, J.W., Lee, R.J., Lee, Y.J., Lee, S.H., Kim, S.Y., Jeong, K.J., Development of a new platform for secretory production of recombinant proteins in Corynebacterium glutamicum. Biotechnol.Bioeng 113 (2016), 163–172.
    • (2016) Biotechnol.Bioeng , vol.113 , pp. 163-172
    • Yim, S.S.1    Choi, J.W.2    Lee, R.J.3    Lee, Y.J.4    Lee, S.H.5    Kim, S.Y.6    Jeong, K.J.7
  • 69
    • 77955559551 scopus 로고    scopus 로고
    • Screening for improved activity of a transglutaminase from Streptomyces mobaraensis created by a novel rational mutagenesis and random mutagenesis
    • Yokoyama, K., Utsumi, H., Nakamura, T., Ogaya, D., Shimba, N., Suzuki, E., Taguchi, S., Screening for improved activity of a transglutaminase from Streptomyces mobaraensis created by a novel rational mutagenesis and random mutagenesis. Appl. Microbiol. Biotechnol. 87 (2010), 2087–2096.
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 2087-2096
    • Yokoyama, K.1    Utsumi, H.2    Nakamura, T.3    Ogaya, D.4    Shimba, N.5    Suzuki, E.6    Taguchi, S.7
  • 70
    • 84945545221 scopus 로고    scopus 로고
    • Construction of a novel twin-arginine translocation (Tat)-dependent type expression vector for secretory production of heterologous proteins in Corynebacterium glutamicum
    • Zhang, L., Lia, H., Xu, D., Construction of a novel twin-arginine translocation (Tat)-dependent type expression vector for secretory production of heterologous proteins in Corynebacterium glutamicum. Plasmid 82 (2015), 50–55.
    • (2015) Plasmid , vol.82 , pp. 50-55
    • Zhang, L.1    Lia, H.2    Xu, D.3
  • 71
    • 49449107199 scopus 로고    scopus 로고
    • Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state
    • Zuber, B., Chami, M., Houssin, C., Dubochet, J., Griffiths, G., Daffé, M., Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state. J. Bacteriol. 190 (2008), 5672–5680.
    • (2008) J. Bacteriol. , vol.190 , pp. 5672-5680
    • Zuber, B.1    Chami, M.2    Houssin, C.3    Dubochet, J.4    Griffiths, G.5    Daffé, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.