메뉴 건너뛰기




Volumn 1843, Issue 8, 2014, Pages 1750-1761

Protein secretion biotechnology in Gram-positive bacteria with special emphasis on Streptomyces lividans

Author keywords

Industrial biotechnology; Recombinant protein secretion; Strain optimization; Streptomyces; Systems biology

Indexed keywords

BACTERIAL PROTEIN; PHAGE SHOCK PROTEIN; PROTEIN ESX1; PROTEIN SECA; SIGNAL PEPTIDASE; SIGNAL PEPTIDE; SIGNAL RECOGNITION PARTICLE; TRANSACTIVATOR PROTEIN; TRANSLOCON; UNCLASSIFIED DRUG;

EID: 84902290726     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.12.023     Document Type: Review
Times cited : (71)

References (163)
  • 2
    • 14844317367 scopus 로고    scopus 로고
    • Secretory expression of thermostable T1 lipase through bacteriocin release protein
    • Rahman R., Leow T.C., Basri M., Salleh A.B. Secretory expression of thermostable T1 lipase through bacteriocin release protein. Protein Expr. Purif. 2005, 40:411-416.
    • (2005) Protein Expr. Purif. , vol.40 , pp. 411-416
    • Rahman, R.1    Leow, T.C.2    Basri, M.3    Salleh, A.B.4
  • 3
    • 35748944106 scopus 로고    scopus 로고
    • Increasing the secretion ability of the kil gene for recombinant proteins in Escherichia coli by using a strong stationary-phase promoter
    • Beshay U., Miksch G., Friehs K., Flaschel E. Increasing the secretion ability of the kil gene for recombinant proteins in Escherichia coli by using a strong stationary-phase promoter. Biotechnol. Lett. 2007, 29:1893-1901.
    • (2007) Biotechnol. Lett. , vol.29 , pp. 1893-1901
    • Beshay, U.1    Miksch, G.2    Friehs, K.3    Flaschel, E.4
  • 4
    • 77952516669 scopus 로고    scopus 로고
    • Secretory production of recombinant proteins in Escherichia coli
    • Yoon S.H., Kim S.K., Kim J.F. Secretory production of recombinant proteins in Escherichia coli. Recent Patents Biotechnol. 2010, 4:23-29.
    • (2010) Recent Patents Biotechnol. , vol.4 , pp. 23-29
    • Yoon, S.H.1    Kim, S.K.2    Kim, J.F.3
  • 5
    • 30544435865 scopus 로고    scopus 로고
    • Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli
    • Zhang G.J., Brokx S., Weiner J.H. Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli. Nat. Biotechnol. 2006, 24:100-104.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 100-104
    • Zhang, G.J.1    Brokx, S.2    Weiner, J.H.3
  • 6
    • 77957354322 scopus 로고    scopus 로고
    • Extracellular production of recombinant proteins using bacterial autotransporters
    • Jong W.S.P., Sauri A., Luirink J. Extracellular production of recombinant proteins using bacterial autotransporters. Curr. Opin. Biotechnol. 2010, 21:646-652.
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 646-652
    • Jong, W.S.P.1    Sauri, A.2    Luirink, J.3
  • 8
    • 70350722394 scopus 로고    scopus 로고
    • Genomic basis for natural product biosynthetic diversity in the actinomycetes
    • Nett M., Ikeda H., Moore B.S. Genomic basis for natural product biosynthetic diversity in the actinomycetes. Nat. Prod. Rep. 2009, 26:1362-1384.
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 1362-1384
    • Nett, M.1    Ikeda, H.2    Moore, B.S.3
  • 9
    • 80052077061 scopus 로고    scopus 로고
    • The regulation of the secondary metabolism of Streptomyces: new links and experimental advances
    • van Wezel G.P., McDowall K.J. The regulation of the secondary metabolism of Streptomyces: new links and experimental advances. Nat. Prod. Rep. 2011, 28:1311-1333.
    • (2011) Nat. Prod. Rep. , vol.28 , pp. 1311-1333
    • van Wezel, G.P.1    McDowall, K.J.2
  • 11
    • 0029111794 scopus 로고
    • A cellulase xylanase-negative mutant of Streptomyces lividans 1326 defective in cellobiose and xylobioase uptakes is mutated in a gene encoding a protein homologous to ATP-binding proteins
    • Hurtubise Y., Shareck F., Kluepfel D., Morosoli R. A cellulase xylanase-negative mutant of Streptomyces lividans 1326 defective in cellobiose and xylobioase uptakes is mutated in a gene encoding a protein homologous to ATP-binding proteins. Mol. Microbiol. 1995, 17:367-377.
    • (1995) Mol. Microbiol. , vol.17 , pp. 367-377
    • Hurtubise, Y.1    Shareck, F.2    Kluepfel, D.3    Morosoli, R.4
  • 12
    • 0001494267 scopus 로고
    • Extracellular enzyme-activities during lignocellulose degradation by Streptomyces spp. - a comparative study of wild-type and genetically manipulated strains
    • Ramachandra M., Crawford D.L., Pometto A.L. Extracellular enzyme-activities during lignocellulose degradation by Streptomyces spp. - a comparative study of wild-type and genetically manipulated strains. Appl. Environ. Microbiol. 1987, 53:2754-2760.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 2754-2760
    • Ramachandra, M.1    Crawford, D.L.2    Pometto, A.L.3
  • 13
    • 0042063909 scopus 로고    scopus 로고
    • Fusion of family 2b carbohydrate-binding module increases the catalytic activity of a xylanase from Thermotoga maritima to soluble xylan
    • Kittur F.S., Mangala S.L., Abu Rus'd A., Kitaoka M., Tsujibo H., Hayashi K. Fusion of family 2b carbohydrate-binding module increases the catalytic activity of a xylanase from Thermotoga maritima to soluble xylan. FEBS Lett. 2003, 549:147-151.
    • (2003) FEBS Lett. , vol.549 , pp. 147-151
    • Kittur, F.S.1    Mangala, S.L.2    Abu Rus'd, A.3    Kitaoka, M.4    Tsujibo, H.5    Hayashi, K.6
  • 15
    • 57649181724 scopus 로고    scopus 로고
    • Flanking signal and mature peptide residues influence signal peptide cleavage
    • Choo K.H., Ranganathan S. Flanking signal and mature peptide residues influence signal peptide cleavage. BMC Bioinforma. 2008, 9.
    • (2008) BMC Bioinforma. , vol.9
    • Choo, K.H.1    Ranganathan, S.2
  • 18
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen T.N., Brunak S., von Heijne G., Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 2011, 8:785-786.
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 19
    • 0034697156 scopus 로고    scopus 로고
    • The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli
    • Stanley N.R., Palmer T., Berks B.C. The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli. J. Biol. Chem. 2000, 275:11591-11596.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 20
    • 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. Microbiol.-UK 2009, 155:741-750.
    • (2009) Microbiol.-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
  • 21
    • 0036038940 scopus 로고    scopus 로고
    • Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway
    • Rose R.W., Bruser T., Kissinger J.C., Pohlschroder M. Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway. Mol. Microbiol. 2002, 45:943-950.
    • (2002) Mol. Microbiol. , vol.45 , pp. 943-950
    • Rose, R.W.1    Bruser, T.2    Kissinger, J.C.3    Pohlschroder, M.4
  • 23
    • 78149257874 scopus 로고    scopus 로고
    • Combined prediction of Tat and Sec signal peptides with hidden Markov models
    • Bagos P.G., Nikolaou E.P., Liakopoulos T.D., Tsirigos K.D. Combined prediction of Tat and Sec signal peptides with hidden Markov models. Bioinformatics 2010, 26:2811-2817.
    • (2010) Bioinformatics , vol.26 , pp. 2811-2817
    • Bagos, P.G.1    Nikolaou, E.P.2    Liakopoulos, T.D.3    Tsirigos, K.D.4
  • 24
    • 0034751046 scopus 로고    scopus 로고
    • Functional analysis of the Streptomyces lividans type I signal peptidases
    • Geukens N., Parro V., Rivas L.A., Mellado R.P., Anné J. Functional analysis of the Streptomyces lividans type I signal peptidases. Arch. Microbiol. 2001, 176:377-380.
    • (2001) Arch. Microbiol. , vol.176 , pp. 377-380
    • Geukens, N.1    Parro, V.2    Rivas, L.A.3    Mellado, R.P.4    Anné, J.5
  • 25
    • 0036718560 scopus 로고    scopus 로고
    • SipY is the Streptomyces lividans type I signal peptidase exerting a major effect on protein secretion
    • Palacin A., Parro V., Geukens N., Anné J., Mellado R.P. SipY is the Streptomyces lividans type I signal peptidase exerting a major effect on protein secretion. J. Bacteriol. 2002, 184:4875-4880.
    • (2002) J. Bacteriol. , vol.184 , pp. 4875-4880
    • Palacin, A.1    Parro, V.2    Geukens, N.3    Anné, J.4    Mellado, R.P.5
  • 26
    • 84870859321 scopus 로고    scopus 로고
    • Breaking on through to the other side: protein export through the bacterial Sec system
    • Chatzi K.E., Sardis M.F., Karamanou S., Economou A. Breaking on through to the other side: protein export through the bacterial Sec system. Biochem. J. 2013, 449:25-37.
    • (2013) Biochem. J. , vol.449 , pp. 25-37
    • Chatzi, K.E.1    Sardis, M.F.2    Karamanou, S.3    Economou, A.4
  • 27
    • 0141814845 scopus 로고    scopus 로고
    • Streptomyces lividans contains a minimal functional signal recognition particle that is involved in protein secretion
    • Palacin A., de la Fuente R., Valle I., Rivas L.A., Mellado R.P. Streptomyces lividans contains a minimal functional signal recognition particle that is involved in protein secretion. Microbiol.-UK 2003, 149:2435-2442.
    • (2003) Microbiol.-UK , vol.149 , pp. 2435-2442
    • Palacin, A.1    de la Fuente, R.2    Valle, I.3    Rivas, L.A.4    Mellado, R.P.5
  • 28
    • 37549014220 scopus 로고    scopus 로고
    • FtsY affects sporulation and antibiotic production by whiH in Streptomyces coelicolor
    • Shen X.L., Dong H.J., Hou X.P., Guan W.J., Li Y.Q. FtsY affects sporulation and antibiotic production by whiH in Streptomyces coelicolor. Curr. Microbiol. 2008, 56:61-65.
    • (2008) Curr. Microbiol. , vol.56 , pp. 61-65
    • Shen, X.L.1    Dong, H.J.2    Hou, X.P.3    Guan, W.J.4    Li, Y.Q.5
  • 31
    • 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. Microbiol.-UK 2004, 150:21-31.
    • (2004) Microbiol.-UK , vol.150 , pp. 21-31
    • Schaerlaekens, K.1    Van Mellaert, L.2    Lammertyn, E.3    Geukens, N.4    Anné, J.5
  • 32
    • 84869146885 scopus 로고    scopus 로고
    • Co-operation between different targeting pathways during integration of a membrane protein
    • Keller R., de Keyzer J., Driessen A.J.M., Palmer T. Co-operation between different targeting pathways during integration of a membrane protein. J. Cell Biol. 2012, 199:303-315.
    • (2012) J. Cell Biol. , vol.199 , pp. 303-315
    • Keller, R.1    de Keyzer, J.2    Driessen, A.J.M.3    Palmer, T.4
  • 34
    • 27744493918 scopus 로고    scopus 로고
    • The twin-arginine translocation pathway of Mycobactetium smegmatis is functional and required for the export of mycobacterial beta-lactamases
    • McDonough J.A., Hacker K.E., Flores A.R., Pavelka M.S., Braunstein M. The twin-arginine translocation pathway of Mycobactetium smegmatis is functional and required for the export of mycobacterial beta-lactamases. J. Bacteriol. 2005, 187:7667-7679.
    • (2005) J. Bacteriol. , vol.187 , pp. 7667-7679
    • McDonough, J.A.1    Hacker, K.E.2    Flores, A.R.3    Pavelka, M.S.4    Braunstein, M.5
  • 35
    • 0037352234 scopus 로고    scopus 로고
    • Moving folded proteins across the bacterial cell membrane
    • Palmer T., Berks B.C. Moving folded proteins across the bacterial cell membrane. Microbiol.-UK 2003, 149:547-556.
    • (2003) Microbiol.-UK , vol.149 , pp. 547-556
    • Palmer, T.1    Berks, B.C.2
  • 36
    • 22144492215 scopus 로고    scopus 로고
    • Determining the functionality of putative Tat-dependent signal peptides in Streptomyces coelicolor A3(2) by using two different reporter proteins
    • Li H.M., Jacques P.L., Ghinet M.G., Brzezinski R., Morosoli R. Determining the functionality of putative Tat-dependent signal peptides in Streptomyces coelicolor A3(2) by using two different reporter proteins. Microbiol.-UK 2005, 151:2189-2198.
    • (2005) Microbiol.-UK , vol.151 , pp. 2189-2198
    • Li, H.M.1    Jacques, P.L.2    Ghinet, M.G.3    Brzezinski, R.4    Morosoli, R.5
  • 38
    • 0242268398 scopus 로고    scopus 로고
    • Acute infection and macrophage subversion by Mycobacterium tuberculosis require a specialized secretion system
    • Stanley S.A., Raghavan S., Hwang W.W., Cox J.S. Acute infection and macrophage subversion by Mycobacterium tuberculosis require a specialized secretion system. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:13001-13006.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13001-13006
    • Stanley, S.A.1    Raghavan, S.2    Hwang, W.W.3    Cox, J.S.4
  • 39
    • 14544279302 scopus 로고    scopus 로고
    • A protein secretion pathway critical for Mycobacterium tuberculosis virulence is conserved and functional in Mycobacterium smegmatis
    • Converse S.E., Cox J.S. A protein secretion pathway critical for Mycobacterium tuberculosis virulence is conserved and functional in Mycobacterium smegmatis. J. Bacteriol. 2005, 187:1238-1245.
    • (2005) J. Bacteriol. , vol.187 , pp. 1238-1245
    • Converse, S.E.1    Cox, J.S.2
  • 41
    • 0036568776 scopus 로고    scopus 로고
    • The ESAT-6/WXG100 superfamily - and a new Gram-positive secretion system?
    • Pallen M.J. The ESAT-6/WXG100 superfamily - and a new Gram-positive secretion system?. Trends Microbiol. 2002, 10:209-212.
    • (2002) Trends Microbiol. , vol.10 , pp. 209-212
    • Pallen, M.J.1
  • 42
    • 84871791448 scopus 로고    scopus 로고
    • The ESX/type VII secretion system modulates development, but not virulence, of the plant pathogen Streptomyces scabies
    • Fyans J.K., Bignell D., Loria R., Toth I., Palmer T. The ESX/type VII secretion system modulates development, but not virulence, of the plant pathogen Streptomyces scabies. Mol. Plant Pathol. 2013, 14:119-130.
    • (2013) Mol. Plant Pathol. , vol.14 , pp. 119-130
    • Fyans, J.K.1    Bignell, D.2    Loria, R.3    Toth, I.4    Palmer, T.5
  • 43
    • 77953181571 scopus 로고    scopus 로고
    • A heterodimer of EsxA and EsxB is involved in sporulation and is secreted by a type VII secretion system in Streptomyces coelicolor
    • San Roman S.A., Facey P.D., Fernandez-Martinez L., Rodriguez C., Vallin C., Del Sol R., Dyson P. A heterodimer of EsxA and EsxB is involved in sporulation and is secreted by a type VII secretion system in Streptomyces coelicolor. Microbiol.-UK 2010, 156:1719-1729.
    • (2010) Microbiol.-UK , vol.156 , pp. 1719-1729
    • San Roman, S.A.1    Facey, P.D.2    Fernandez-Martinez, L.3    Rodriguez, C.4    Vallin, C.5    Del Sol, R.6    Dyson, P.7
  • 48
    • 0037208813 scopus 로고    scopus 로고
    • Use of tRNA-supplemented host strains for expression of heterologous genes in E. coli
    • Carstens C.P. Use of tRNA-supplemented host strains for expression of heterologous genes in E. coli. Methods Mol. Biol. (Clifton, N.J.) 2003, 205:225-233.
    • (2003) Methods Mol. Biol. (Clifton, N.J.) , vol.205 , pp. 225-233
    • Carstens, C.P.1
  • 49
    • 63849189906 scopus 로고    scopus 로고
    • Secretory production of recombinant proteins by Streptomyces
    • Vrancken K., Anné J. Secretory production of recombinant proteins by Streptomyces. Future Microbiol. 2009, 4:181-188.
    • (2009) Future Microbiol. , vol.4 , pp. 181-188
    • Vrancken, K.1    Anné, J.2
  • 50
    • 67650128120 scopus 로고    scopus 로고
    • New approach to achieve high-level secretory expression of heterologous proteins by using Tat signal peptide
    • Li Y.D., Zhou Z., Lv L.X., Hou X.P., Li Y.Q. New approach to achieve high-level secretory expression of heterologous proteins by using Tat signal peptide. Protein Pept. Lett. 2009, 16:706-710.
    • (2009) Protein Pept. Lett. , vol.16 , pp. 706-710
    • Li, Y.D.1    Zhou, Z.2    Lv, L.X.3    Hou, X.P.4    Li, Y.Q.5
  • 51
    • 79953210780 scopus 로고    scopus 로고
    • Metagenomic analyses: past and future trends
    • Simon C., Daniel R. Metagenomic analyses: past and future trends. Appl. Environ. Microbiol. 2011, 77:1153-1161.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 1153-1161
    • Simon, C.1    Daniel, R.2
  • 52
    • 28544451203 scopus 로고    scopus 로고
    • Environments shape the nucleotide composition of genomes
    • Foerstner K.U., von Mering C., Hooper S.D., Bork P. Environments shape the nucleotide composition of genomes. EMBO Rep. 2005, 6:1208-1213.
    • (2005) EMBO Rep. , vol.6 , pp. 1208-1213
    • Foerstner, K.U.1    von Mering, C.2    Hooper, S.D.3    Bork, P.4
  • 54
  • 55
    • 0030903569 scopus 로고    scopus 로고
    • Evaluation of a novel subtilisin inhibitor gene and mutant derivatives for the expression and secretion of mouse tumor necrosis factor alpha by Streptomyces lividans
    • Lammertyn E., VanMellaert L., Schacht S., Dillen C., Sablon E., VanBroekhoven A., Anné J. Evaluation of a novel subtilisin inhibitor gene and mutant derivatives for the expression and secretion of mouse tumor necrosis factor alpha by Streptomyces lividans. Appl. Environ. Microbiol. 1997, 63:1808-1813.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1808-1813
    • Lammertyn, E.1    VanMellaert, L.2    Schacht, S.3    Dillen, C.4    Sablon, E.5    VanBroekhoven, A.6    Anné, J.7
  • 56
    • 0028079724 scopus 로고
    • The messenger RNA for the 23s ribosomal-RNA methylase encoded by the ermE gene of Saccharopolyspora erythraea is translated in the absence of a conventional ribosome binding site
    • Bibb M.J., White J., Ward J.M., Janssen G.R. The messenger RNA for the 23s ribosomal-RNA methylase encoded by the ermE gene of Saccharopolyspora erythraea is translated in the absence of a conventional ribosome binding site. Mol. Microbiol. 1994, 14:533-545.
    • (1994) Mol. Microbiol. , vol.14 , pp. 533-545
    • Bibb, M.J.1    White, J.2    Ward, J.M.3    Janssen, G.R.4
  • 58
    • 0032541316 scopus 로고    scopus 로고
    • Construction of new vectors for high-level expression in actinomycetes
    • Rowe C.J., Cortes J., Gaisser S., Staunton J., Leadley P.F. Construction of new vectors for high-level expression in actinomycetes. Gene 1998, 216:215-223.
    • (1998) Gene , vol.216 , pp. 215-223
    • Rowe, C.J.1    Cortes, J.2    Gaisser, S.3    Staunton, J.4    Leadley, P.F.5
  • 62
    • 0031726240 scopus 로고    scopus 로고
    • An inducible expression system permitting the efficient purification of a recombinant antigen from Mycobacterium smegmatis
    • Triccas J.A., Parish T., Britton W.J., Gicquel B. An inducible expression system permitting the efficient purification of a recombinant antigen from Mycobacterium smegmatis. FEMS Microbiol. Lett. 1998, 167:151-156.
    • (1998) FEMS Microbiol. Lett. , vol.167 , pp. 151-156
    • Triccas, J.A.1    Parish, T.2    Britton, W.J.3    Gicquel, B.4
  • 63
    • 0024515525 scopus 로고
    • Thiostrepton-induced gene-expression in Strepomyces lividans
    • Murakami T., Holt T.G., Thompson C.J. Thiostrepton-induced gene-expression in Strepomyces lividans. J. Bacteriol. 1989, 171:1459-1466.
    • (1989) J. Bacteriol. , vol.171 , pp. 1459-1466
    • Murakami, T.1    Holt, T.G.2    Thompson, C.J.3
  • 66
  • 68
    • 44849091539 scopus 로고    scopus 로고
    • Heterologous protein secretion by Lactobacillus plantarum using homologous signal peptides
    • Mathiesen G., Sveen A., Piard J.C., Axelsson L., Eijsink V.G.H. Heterologous protein secretion by Lactobacillus plantarum using homologous signal peptides. J. Appl. Microbiol. 2008, 105:215-226.
    • (2008) J. Appl. Microbiol. , vol.105 , pp. 215-226
    • Mathiesen, G.1    Sveen, A.2    Piard, J.C.3    Axelsson, L.4    Eijsink, V.G.H.5
  • 69
    • 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. 2006, 362:393-402.
    • (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
  • 70
    • 0032032192 scopus 로고    scopus 로고
    • Modifications of Streptomyces signal peptides and their effects on protein production and secretion
    • Lammertyn E., Anné J. Modifications of Streptomyces signal peptides and their effects on protein production and secretion. FEMS Microbiol. Lett. 1998, 160:1-10.
    • (1998) FEMS Microbiol. Lett. , vol.160 , pp. 1-10
    • Lammertyn, E.1    Anné, J.2
  • 71
    • 77952882027 scopus 로고    scopus 로고
    • Improvement of Sec-dependent secretion of a heterologous model protein in Bacillus subtilis by saturation mutagenesis of the N-domain of the AmyE signal peptide
    • Caspers M., Brockmeier U., Degering C., Eggert T., Freudl R. Improvement of Sec-dependent secretion of a heterologous model protein in Bacillus subtilis by saturation mutagenesis of the N-domain of the AmyE signal peptide. Appl. Microbiol. Biotechnol. 2010, 86:1877-1885.
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 1877-1885
    • Caspers, M.1    Brockmeier, U.2    Degering, C.3    Eggert, T.4    Freudl, R.5
  • 72
    • 84871866528 scopus 로고    scopus 로고
    • Engineering signal peptides for enhanced protein secretion from Lactococcus lactis
    • Ng D.T.W., Sarkar C.A. Engineering signal peptides for enhanced protein secretion from Lactococcus lactis. Appl. Environ. Microbiol. 2013, 79:347-356.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 347-356
    • Ng, D.T.W.1    Sarkar, C.A.2
  • 73
    • 84862577056 scopus 로고    scopus 로고
    • Membrane proteases in the bacterial protein secretion and quality control pathway
    • Dalbey R.E., Wang P., van Dijl J.M. Membrane proteases in the bacterial protein secretion and quality control pathway. Microbiol. Mol. Biol. Rev. 2012, 76:311-330.
    • (2012) Microbiol. Mol. Biol. Rev. , vol.76 , pp. 311-330
    • Dalbey, R.E.1    Wang, P.2    van Dijl, J.M.3
  • 76
    • 0027401020 scopus 로고
    • Protein secretion in Bacillus species
    • Simonen M., Palva I. Protein secretion in Bacillus species. Microbiol. Rev. 1993, 57:109-137.
    • (1993) Microbiol. Rev. , vol.57 , pp. 109-137
    • Simonen, M.1    Palva, I.2
  • 77
    • 35848952765 scopus 로고    scopus 로고
    • Protein secretion in gram-negative bacteria via the autotransporter pathway
    • Dautin N., Bernstein H.D. Protein secretion in gram-negative bacteria via the autotransporter pathway. Ann. Rev. Microbiol. 2007, 61:89-112.
    • (2007) Ann. Rev. Microbiol. , vol.61 , pp. 89-112
    • Dautin, N.1    Bernstein, H.D.2
  • 78
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome
    • Tjalsma H., Bolhuis A., Jongbloed J.D.H., Bron S., van Dijl J.M. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol. Mol. Biol. Rev. 2000, 64:515-547.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.H.3    Bron, S.4    van Dijl, J.M.5
  • 79
    • 8844278305 scopus 로고    scopus 로고
    • Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism
    • Westers L., Westers H., Quax W.J. Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism. BBA-Mol. Cell Res. 2004, 1694:299-310.
    • (2004) BBA-Mol. Cell Res. , vol.1694 , pp. 299-310
    • Westers, L.1    Westers, H.2    Quax, W.J.3
  • 81
    • 25144465928 scopus 로고    scopus 로고
    • Coexpression of the type I signal peptidase gene sipM increases recombinant protein production and export in Bacillus megaterium MS941
    • Malten M., Nahrstedt H., Meinhardt F., Jahn D. Coexpression of the type I signal peptidase gene sipM increases recombinant protein production and export in Bacillus megaterium MS941. Biotechnol. Bioeng. 2005, 91:616-621.
    • (2005) Biotechnol. Bioeng. , vol.91 , pp. 616-621
    • Malten, M.1    Nahrstedt, H.2    Meinhardt, F.3    Jahn, D.4
  • 82
    • 0025869932 scopus 로고
    • Signal peptidase I overproduction results in increased efficiencies of export and maturation of hybrid secretory proteins in Escherichia coli
    • van Dijl J.M., de Jong A., Smith H., Bron S., Venema G. Signal peptidase I overproduction results in increased efficiencies of export and maturation of hybrid secretory proteins in Escherichia coli. Mol. Gen. Genet. MGG 1991, 227:40-48.
    • (1991) Mol. Gen. Genet. MGG , vol.227 , pp. 40-48
    • van Dijl, J.M.1    de Jong, A.2    Smith, H.3    Bron, S.4    Venema, G.5
  • 83
    • 0033573986 scopus 로고    scopus 로고
    • A bacterial signal peptidase enhances processing of a recombinant single chain antibody fragment in insect cells
    • Ailor E., Pathmanathan J., Jongbloed J.D.H., Betenbaugh M.J. A bacterial signal peptidase enhances processing of a recombinant single chain antibody fragment in insect cells. Biochem. Biophys. Res. Commun. 1999, 255:444-450.
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 444-450
    • Ailor, E.1    Pathmanathan, J.2    Jongbloed, J.D.H.3    Betenbaugh, M.J.4
  • 84
    • 79952443838 scopus 로고    scopus 로고
    • Consequences of the overexpression of a eukaryotic membrane protein, the human KDEL receptor, in Escherichia coli
    • Klepsch M.M., Persson J.O., de Gier J.W.L. Consequences of the overexpression of a eukaryotic membrane protein, the human KDEL receptor, in Escherichia coli. J. Mol. Biol. 2011, 407:532-542.
    • (2011) J. Mol. Biol. , vol.407 , pp. 532-542
    • Klepsch, M.M.1    Persson, J.O.2    de Gier, J.W.L.3
  • 85
    • 84874768785 scopus 로고    scopus 로고
    • Optimizing heterologous protein production in the periplasm of E. coli by regulating gene expression levels
    • Schlegel S., Rujas E., Ytterberg A.J., Zubarev R.A., Luirink J., de Gier J.W. Optimizing heterologous protein production in the periplasm of E. coli by regulating gene expression levels. Microb. Cell Fact. 2013, 12:24.
    • (2013) Microb. Cell Fact. , vol.12 , pp. 24
    • Schlegel, S.1    Rujas, E.2    Ytterberg, A.J.3    Zubarev, R.A.4    Luirink, J.5    de Gier, J.W.6
  • 86
    • 0033064845 scopus 로고    scopus 로고
    • Differential dependence of levansucrase and alpha-amylase secretion on SecA (Div) during the exponential phase of growth of Bacillus subtilis
    • Leloup L., Driessen A.J.M., Freudl R., Chambert R., Petit-Glatron M.F. Differential dependence of levansucrase and alpha-amylase secretion on SecA (Div) during the exponential phase of growth of Bacillus subtilis. J. Bacteriol. 1999, 181:1820-1826.
    • (1999) J. Bacteriol. , vol.181 , pp. 1820-1826
    • Leloup, L.1    Driessen, A.J.M.2    Freudl, R.3    Chambert, R.4    Petit-Glatron, M.F.5
  • 87
    • 77958097022 scopus 로고    scopus 로고
    • Enhanced extracellular production of heterologous proteins in Bacillus subtilis by deleting the C-terminal region of the SecA secretory machinery
    • Kakeshtia H., Kageyama Y., Ara K., Ozaki K., Nakamura K. Enhanced extracellular production of heterologous proteins in Bacillus subtilis by deleting the C-terminal region of the SecA secretory machinery. Mol. Biotechnol. 2010, 46:250-257.
    • (2010) Mol. Biotechnol. , vol.46 , pp. 250-257
    • Kakeshtia, H.1    Kageyama, Y.2    Ara, K.3    Ozaki, K.4    Nakamura, K.5
  • 88
    • 84862929304 scopus 로고    scopus 로고
    • Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis
    • Diao L.Y., Dong Q.L., Xu Z.H., Yang S., Zhou J.H., Freudl R. Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis. Appl. Environ. Microbiol. 2012, 78:651-659.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 651-659
    • Diao, L.Y.1    Dong, Q.L.2    Xu, Z.H.3    Yang, S.4    Zhou, J.H.5    Freudl, R.6
  • 89
    • 84875503513 scopus 로고    scopus 로고
    • Construction of an artificial secYEG operon allowing high level secretion of alpha-amylase
    • Mulder K.C.L., Bandola J., Schumann W. Construction of an artificial secYEG operon allowing high level secretion of alpha-amylase. Protein Expr. Purif. 2013, 89:92-96.
    • (2013) Protein Expr. Purif. , vol.89 , pp. 92-96
    • Mulder, K.C.L.1    Bandola, J.2    Schumann, W.3
  • 90
    • 0035873543 scopus 로고    scopus 로고
    • Functional reconstitution of bacterial Tat translocation in vitro
    • Yahr T.L., Wickner W.T. Functional reconstitution of bacterial Tat translocation in vitro. EMBO J. 2001, 20:2472-2479.
    • (2001) EMBO J. , vol.20 , pp. 2472-2479
    • Yahr, T.L.1    Wickner, W.T.2
  • 91
    • 0346655242 scopus 로고    scopus 로고
    • Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway
    • DeLisa M.P., Lee P., Palmer T., Georgiou G. Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway. J. Bacteriol. 2004, 186:366-373.
    • (2004) J. Bacteriol. , vol.186 , pp. 366-373
    • DeLisa, M.P.1    Lee, P.2    Palmer, T.3    Georgiou, G.4
  • 92
    • 0037414423 scopus 로고    scopus 로고
    • Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli
    • Barrett C.M., Ray N., Thomas J.D., Robinson C., Bolhuis A. Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli. Biochem. Biophys. Res. Commun. 2003, 304:279-284.
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 279-284
    • Barrett, C.M.1    Ray, N.2    Thomas, J.D.3    Robinson, C.4    Bolhuis, A.5
  • 93
    • 0033579428 scopus 로고    scopus 로고
    • Sec-independent protein translocation in Escherichia coli - a distinct and pivotal role for the TatB protein
    • Sargent F., Stanley N.R., Berks B.C., Palmer T. Sec-independent protein translocation in Escherichia coli - a distinct and pivotal role for the TatB protein. J. Biol. Chem. 1999, 274:36073-36082.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36073-36082
    • Sargent, F.1    Stanley, N.R.2    Berks, B.C.3    Palmer, T.4
  • 94
  • 95
    • 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. 2009, 75:603-607.
    • (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
  • 96
    • 22644441730 scopus 로고    scopus 로고
    • The phage-shock-protein response
    • Darwin A.J. The phage-shock-protein response. Mol. Microbiol. 2005, 57:621-628.
    • (2005) Mol. Microbiol. , vol.57 , pp. 621-628
    • Darwin, A.J.1
  • 97
  • 98
    • 0242575006 scopus 로고    scopus 로고
    • Secretion defects that activate the phage shock response of Escherichia coli
    • Jones S.E., Lloyd L.J., Tan K.K., Buck M. Secretion defects that activate the phage shock response of Escherichia coli. J. Bacteriol. 2003, 185:6707-6711.
    • (2003) J. Bacteriol. , vol.185 , pp. 6707-6711
    • Jones, S.E.1    Lloyd, L.J.2    Tan, K.K.3    Buck, M.4
  • 99
    • 84865031049 scopus 로고    scopus 로고
    • The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli
    • Mehner D., Osadnik H., Lunsdorf H., Bruser T. The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli. J. Biol. Chem. 2012, 287:27834-27842.
    • (2012) J. Biol. Chem. , vol.287 , pp. 27834-27842
    • Mehner, D.1    Osadnik, H.2    Lunsdorf, H.3    Bruser, T.4
  • 100
    • 46249106362 scopus 로고    scopus 로고
    • Proteomic analysis of Haloferax volcanii reveals salinity-mediated regulation of the stress response protein PspA
    • Bidle K.A., Kirkland P.A., Nannen J.L., Maupin-Furlow J.A. Proteomic analysis of Haloferax volcanii reveals salinity-mediated regulation of the stress response protein PspA. Microbiol.-SGM 2008, 154:1436-1443.
    • (2008) Microbiol.-SGM , vol.154 , pp. 1436-1443
    • Bidle, K.A.1    Kirkland, P.A.2    Nannen, J.L.3    Maupin-Furlow, J.A.4
  • 101
    • 34247185926 scopus 로고    scopus 로고
    • The chloroplast HSP70B-CDJ2-CGE1 chaperones catalyse assembly and disassembly of VIPP1 oligomers in Chlamydomonas
    • Liu C.M., Willmund F., Golecki J.R., Cacace S., Hess B., Markert C., Schroda M. The chloroplast HSP70B-CDJ2-CGE1 chaperones catalyse assembly and disassembly of VIPP1 oligomers in Chlamydomonas. Plant J. 2007, 50:265-277.
    • (2007) Plant J. , vol.50 , pp. 265-277
    • Liu, C.M.1    Willmund, F.2    Golecki, J.R.3    Cacace, S.4    Hess, B.5    Markert, C.6    Schroda, M.7
  • 102
    • 79959962403 scopus 로고    scopus 로고
    • Enhancement of excretory production of an exoglucanase from Escherichia coli with phage shock protein A (PspA) overexpression
    • Wang Y.Y., Fu Z.B., Ng K.L., Lam C.C., Chan A.K.N., Sze K.F., Wong W.K.R. Enhancement of excretory production of an exoglucanase from Escherichia coli with phage shock protein A (PspA) overexpression. J. Microbiol. Biotechnol. 2011, 21:637-645.
    • (2011) J. Microbiol. Biotechnol. , vol.21 , pp. 637-645
    • Wang, Y.Y.1    Fu, Z.B.2    Ng, K.L.3    Lam, C.C.4    Chan, A.K.N.5    Sze, K.F.6    Wong, W.K.R.7
  • 104
    • 0030028862 scopus 로고    scopus 로고
    • Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the protonmotive force under stress conditions
    • Kleerebezem M., Crielaard W., Tommassen J. Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the protonmotive force under stress conditions. EMBO J. 1996, 15:162-171.
    • (1996) EMBO J. , vol.15 , pp. 162-171
    • Kleerebezem, M.1    Crielaard, W.2    Tommassen, J.3
  • 106
  • 107
    • 17644401443 scopus 로고    scopus 로고
    • Compensatory role of PspA, a member of the phage shock protein operon, in rpoE mutant Salmonella enterica serovar Typhimurium
    • Becker L.A., Bang I.S., Crouch M.L., Fang F.C. Compensatory role of PspA, a member of the phage shock protein operon, in rpoE mutant Salmonella enterica serovar Typhimurium. Mol. Microbiol. 2005, 56:1004-1016.
    • (2005) Mol. Microbiol. , vol.56 , pp. 1004-1016
    • Becker, L.A.1    Bang, I.S.2    Crouch, M.L.3    Fang, F.C.4
  • 108
    • 15344343162 scopus 로고    scopus 로고
    • Role of the extracytoplasmic function protein family sigma factor RpoE in metal resistance of Escherichia coli
    • Egler M., Grosse C., Grass G., Nies D.H. Role of the extracytoplasmic function protein family sigma factor RpoE in metal resistance of Escherichia coli. J. Bacteriol. 2005, 187:2297-2307.
    • (2005) J. Bacteriol. , vol.187 , pp. 2297-2307
    • Egler, M.1    Grosse, C.2    Grass, G.3    Nies, D.H.4
  • 110
    • 84866493378 scopus 로고    scopus 로고
    • On the influence of overexpression of phosphoenolpyruvate carboxykinase in Streptomyces lividans on growth and production of human tumour necrosis factor-alpha
    • Lule I., Maldonado B., D'Huys P.J., Van Mellaert L., Van Impe J., Bernaerts K., Anne J. On the influence of overexpression of phosphoenolpyruvate carboxykinase in Streptomyces lividans on growth and production of human tumour necrosis factor-alpha. Appl. Microbiol. Biotechnol. 2012, 96:367-372.
    • (2012) Appl. Microbiol. Biotechnol. , vol.96 , pp. 367-372
    • Lule, I.1    Maldonado, B.2    D'Huys, P.J.3    Van Mellaert, L.4    Van Impe, J.5    Bernaerts, K.6    Anne, J.7
  • 111
    • 0028801765 scopus 로고
    • Metabolic load and heterologous gene-expression
    • Glick B.R. Metabolic load and heterologous gene-expression. Biotechnol. Adv. 1995, 13:247-261.
    • (1995) Biotechnol. Adv. , vol.13 , pp. 247-261
    • Glick, B.R.1
  • 112
    • 79959227594 scopus 로고    scopus 로고
    • Carbon metabolism limits recombinant protein production in Pichia pastoris
    • Heyland J., Fu J.A., Blank L.M., Schmid A. Carbon metabolism limits recombinant protein production in Pichia pastoris. Biotechnol. Bioeng. 2011, 108:1942-1953.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 1942-1953
    • Heyland, J.1    Fu, J.A.2    Blank, L.M.3    Schmid, A.4
  • 114
    • 43949110569 scopus 로고    scopus 로고
    • Hyphenated mass spectrometry in the analysis of the central carbon metabolism
    • Timischl B., Dettmer K., Oefner P.J. Hyphenated mass spectrometry in the analysis of the central carbon metabolism. Anal. Bioanal. Chem. 2008, 391:895-898.
    • (2008) Anal. Bioanal. Chem. , vol.391 , pp. 895-898
    • Timischl, B.1    Dettmer, K.2    Oefner, P.J.3
  • 115
    • 41049099137 scopus 로고    scopus 로고
    • Current and emerging mass-spectrometry technologies for metabolomics
    • Bedair M., Sumner L.W. Current and emerging mass-spectrometry technologies for metabolomics. Trends Anal. Chem. 2008, 27:238-250.
    • (2008) Trends Anal. Chem. , vol.27 , pp. 238-250
    • Bedair, M.1    Sumner, L.W.2
  • 116
    • 48749132804 scopus 로고    scopus 로고
    • Analytical strategies for LC-MS-based targeted metabolomics
    • Lu W., Bennett B.D., Rabinowitz J.D. Analytical strategies for LC-MS-based targeted metabolomics. J. Chromatogr. 2008, 871:236-242.
    • (2008) J. Chromatogr. , vol.871 , pp. 236-242
    • Lu, W.1    Bennett, B.D.2    Rabinowitz, J.D.3
  • 117
    • 20944448468 scopus 로고    scopus 로고
    • Microbial metabolomics: replacing trial-and-error by the unbiased selection and ranking of targets
    • van der Werf M.J., Jellema R.H., Hankemeier T. Microbial metabolomics: replacing trial-and-error by the unbiased selection and ranking of targets. J. Ind. Microbiol. Biotechnol. 2005, 32:234-252.
    • (2005) J. Ind. Microbiol. Biotechnol. , vol.32 , pp. 234-252
    • van der Werf, M.J.1    Jellema, R.H.2    Hankemeier, T.3
  • 119
    • 77951618585 scopus 로고    scopus 로고
    • Assessment of adaptive focused acoustics versus manual vortex/freeze-thaw for intracellular metabolite extraction from Streptomyces lividans producing recombinant proteins using GC-MS and multi-block principal component analysis
    • Kassama Y., Xu Y., Dunn W.B., Geukens N., Anne J., Goodacre R. Assessment of adaptive focused acoustics versus manual vortex/freeze-thaw for intracellular metabolite extraction from Streptomyces lividans producing recombinant proteins using GC-MS and multi-block principal component analysis. Analyst 2010, 135:934-942.
    • (2010) Analyst , vol.135 , pp. 934-942
    • Kassama, Y.1    Xu, Y.2    Dunn, W.B.3    Geukens, N.4    Anne, J.5    Goodacre, R.6
  • 121
    • 84862175899 scopus 로고    scopus 로고
    • Quantitative metabolomics analysis of amino acid metabolism in recombinant Pichia pastoris under different oxygen availability conditions
    • Carnicer M., ten Pierick A., van Dam J., Heijnen J.J., Albiol J., van Gulik W., Ferrer P. Quantitative metabolomics analysis of amino acid metabolism in recombinant Pichia pastoris under different oxygen availability conditions. Microb. Cell Fact. 2012, 11:83.
    • (2012) Microb. Cell Fact. , vol.11 , pp. 83
    • Carnicer, M.1    ten Pierick, A.2    van Dam, J.3    Heijnen, J.J.4    Albiol, J.5    van Gulik, W.6    Ferrer, P.7
  • 122
    • 79951623012 scopus 로고    scopus 로고
    • Metabolic footprint analysis of recombinant Escherichia coli strains during fed-batch fermentations
    • Carneiro S., Villas-Boas S.G., Ferreira E.C., Rocha I. Metabolic footprint analysis of recombinant Escherichia coli strains during fed-batch fermentations. Mol. Biosyst. 2011, 7:899-910.
    • (2011) Mol. Biosyst. , vol.7 , pp. 899-910
    • Carneiro, S.1    Villas-Boas, S.G.2    Ferreira, E.C.3    Rocha, I.4
  • 124
    • 39449095000 scopus 로고    scopus 로고
    • Stoichiometric modelling of cell metabolism
    • Llaneras F., Pico J. Stoichiometric modelling of cell metabolism. J. Biosci. Bioeng. 2008, 105:1-11.
    • (2008) J. Biosci. Bioeng. , vol.105 , pp. 1-11
    • Llaneras, F.1    Pico, J.2
  • 126
    • 64549111428 scopus 로고    scopus 로고
    • Yeast systems biotechnology for the production of heterologous proteins
    • Graf A., Dragosits M., Gasser B., Mattanovich D. Yeast systems biotechnology for the production of heterologous proteins. FEMS Yeast Res. 2009, 9:335-348.
    • (2009) FEMS Yeast Res. , vol.9 , pp. 335-348
    • Graf, A.1    Dragosits, M.2    Gasser, B.3    Mattanovich, D.4
  • 127
    • 84878836229 scopus 로고    scopus 로고
    • Systems metabolic engineering in an industrial setting
    • Sagt C.M.J. Systems metabolic engineering in an industrial setting. Appl. Microbiol. Biotechnol. 2013, 97:2319-2326.
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 2319-2326
    • Sagt, C.M.J.1
  • 128
    • 76849116990 scopus 로고    scopus 로고
    • Sense and nonsense from a systems biology approach to microbial recombinant protein production
    • Sevastsyanovich Y.R., Alfasi S.N., Cole J.A. Sense and nonsense from a systems biology approach to microbial recombinant protein production. Biotechnol. Appl. Biochem. 2010, 55:9-28.
    • (2010) Biotechnol. Appl. Biochem. , vol.55 , pp. 9-28
    • Sevastsyanovich, Y.R.1    Alfasi, S.N.2    Cole, J.A.3
  • 129
    • 84855419801 scopus 로고    scopus 로고
    • Integration of in vivo and in silico metabolic fluxes for improvement of recombinant protein production
    • Driouch H., Melzer G., Wittmann C. Integration of in vivo and in silico metabolic fluxes for improvement of recombinant protein production. Metab. Eng. 2012, 14:47-58.
    • (2012) Metab. Eng. , vol.14 , pp. 47-58
    • Driouch, H.1    Melzer, G.2    Wittmann, C.3
  • 131
    • 33747354689 scopus 로고    scopus 로고
    • The use of genome scale metabolic flux variability analysis for process feed formulation based on an investigation of the effects of the zwf mutation on antibiotic production in Streptomyces coelicolor
    • Bushell M.E., Sequeira S.I.P., Khannapho C., Zhao H.J., Chater K.F., Butler M.J., Kierzek A.M., Avignone-Rossa C.A. The use of genome scale metabolic flux variability analysis for process feed formulation based on an investigation of the effects of the zwf mutation on antibiotic production in Streptomyces coelicolor. Enzym. Microb. Technol. 2006, 39:1347-1353.
    • (2006) Enzym. Microb. Technol. , vol.39 , pp. 1347-1353
    • Bushell, M.E.1    Sequeira, S.I.P.2    Khannapho, C.3    Zhao, H.J.4    Chater, K.F.5    Butler, M.J.6    Kierzek, A.M.7    Avignone-Rossa, C.A.8
  • 132
    • 84862796646 scopus 로고    scopus 로고
    • In silico aided metabolic engineering of Streptomyces roseosporus for daptomycin yield improvement
    • Huang D., Wen J.P., Wang G.Y., Yu G.H., Jia X.Q., Chen Y.L. In silico aided metabolic engineering of Streptomyces roseosporus for daptomycin yield improvement. Appl. Microbiol. Biotechnol. 2012, 94:637-649.
    • (2012) Appl. Microbiol. Biotechnol. , vol.94 , pp. 637-649
    • Huang, D.1    Wen, J.P.2    Wang, G.Y.3    Yu, G.H.4    Jia, X.Q.5    Chen, Y.L.6
  • 133
    • 79951846247 scopus 로고    scopus 로고
    • Engineering Streptomyces coelicolor for heterologous expression of secondary metabolite gene clusters
    • Gomez-Escribano J.P., Bibb M.J. Engineering Streptomyces coelicolor for heterologous expression of secondary metabolite gene clusters. Microb. Biotechnol. 2011, 4:207-215.
    • (2011) Microb. Biotechnol. , vol.4 , pp. 207-215
    • Gomez-Escribano, J.P.1    Bibb, M.J.2
  • 134
    • 77249153701 scopus 로고    scopus 로고
    • Genome-minimized Streptomyces host for the heterologous expression of secondary metabolism
    • Komatsua M., Uchiyama T., Omura S., Cane D.E., Ikeda H. Genome-minimized Streptomyces host for the heterologous expression of secondary metabolism. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:2646-2651.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 2646-2651
    • Komatsua, M.1    Uchiyama, T.2    Omura, S.3    Cane, D.E.4    Ikeda, H.5
  • 135
    • 33845911726 scopus 로고    scopus 로고
    • Comparative study on central metabolic fluxes of Bacillus megaterium strains in continuous culture using C-13 labelled substrates
    • Furch T., Hollmann R., Wittmann C., Wang W., Deckwer W.D. Comparative study on central metabolic fluxes of Bacillus megaterium strains in continuous culture using C-13 labelled substrates. Bioproc. Biosyst. Eng. 2007, 30:47-59.
    • (2007) Bioproc. Biosyst. Eng. , vol.30 , pp. 47-59
    • Furch, T.1    Hollmann, R.2    Wittmann, C.3    Wang, W.4    Deckwer, W.D.5
  • 136
    • 35748959651 scopus 로고    scopus 로고
    • Response of fluxome and metabolome to temperature-induced recombinant protein synthesis in Escherichia coli
    • Wittmann C., Weber J., Betiku E., Kroemer J., Boehm D., Rinas U. Response of fluxome and metabolome to temperature-induced recombinant protein synthesis in Escherichia coli. J. Biotechnol. 2007, 132:375-384.
    • (2007) J. Biotechnol. , vol.132 , pp. 375-384
    • Wittmann, C.1    Weber, J.2    Betiku, E.3    Kroemer, J.4    Boehm, D.5    Rinas, U.6
  • 137
    • 64549091131 scopus 로고    scopus 로고
    • Identification of cellular objective for elucidating the physiological state of plasmid-bearing Escherichia coli using genome-scale in silico analysis
    • Ow D.S.W., Lee D.Y., Yap M.G.S., Oh S.K.W. Identification of cellular objective for elucidating the physiological state of plasmid-bearing Escherichia coli using genome-scale in silico analysis. Biotechnol. Progr. 2009, 25:61-67.
    • (2009) Biotechnol. Progr. , vol.25 , pp. 61-67
    • Ow, D.S.W.1    Lee, D.Y.2    Yap, M.G.S.3    Oh, S.K.W.4
  • 139
    • 27744488443 scopus 로고    scopus 로고
    • Applications of metabolic modeling to drive bioprocess development for the production of value-added chemicals
    • Mahadevan R., Burgard A.P., Famili I., Van Dien S., Schilling C.H. Applications of metabolic modeling to drive bioprocess development for the production of value-added chemicals. Biotechnol. Bioproc. Eng. 2005, 10:408-417.
    • (2005) Biotechnol. Bioproc. Eng. , vol.10 , pp. 408-417
    • Mahadevan, R.1    Burgard, A.P.2    Famili, I.3    Van Dien, S.4    Schilling, C.H.5
  • 140
    • 84859891750 scopus 로고    scopus 로고
    • Debottlenecking recombinant protein production in Bacillus megaterium under large-scale conditions-targeted precursor feeding designed from metabolomics
    • Korneli C., Bolten C.J., Godard T., Franco-Lara E., Wittmann C. Debottlenecking recombinant protein production in Bacillus megaterium under large-scale conditions-targeted precursor feeding designed from metabolomics. Biotechnol. Bioeng. 2012, 109:1538-1550.
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 1538-1550
    • Korneli, C.1    Bolten, C.J.2    Godard, T.3    Franco-Lara, E.4    Wittmann, C.5
  • 141
    • 37549014221 scopus 로고    scopus 로고
    • Development of a minimal defined medium for recombinant human interleukin-3 production by Streptomyces lividans 66
    • Nowruzi K., Elkamel A., Scharer J.M., Cossar D., Moo-Young M. Development of a minimal defined medium for recombinant human interleukin-3 production by Streptomyces lividans 66. Biotechnol. Bioeng. 2008, 99:214-222.
    • (2008) Biotechnol. Bioeng. , vol.99 , pp. 214-222
    • Nowruzi, K.1    Elkamel, A.2    Scharer, J.M.3    Cossar, D.4    Moo-Young, M.5
  • 142
    • 39049125071 scopus 로고    scopus 로고
    • Bacillus protein secretion: an unfolding story
    • Harwood C.R., Cranenburgh R. Bacillus protein secretion: an unfolding story. Trends Microbiol. 2008, 16:73-79.
    • (2008) Trends Microbiol. , vol.16 , pp. 73-79
    • Harwood, C.R.1    Cranenburgh, R.2
  • 143
    • 77956107104 scopus 로고    scopus 로고
    • Heterologous protein secretion by Bacillus species: from the cradle to the grave
    • A.I. Laskin, S. Sariaslani, G.M. Gadd (Eds.)
    • Pohl S., Harwood C.R. Heterologous protein secretion by Bacillus species: from the cradle to the grave. Adv. Appl. Microbiol 2010, 73:1-25. A.I. Laskin, S. Sariaslani, G.M. Gadd (Eds.).
    • (2010) Adv. Appl. Microbiol , vol.73 , pp. 1-25
    • Pohl, S.1    Harwood, C.R.2
  • 144
    • 0025906712 scopus 로고
    • A gene (prsa) of Bacillus subtilis involved in a novel, late state of protein export
    • Kontinen V.P., Saris P., Sarvas M. A gene (prsa) of Bacillus subtilis involved in a novel, late state of protein export. Mol. Microbiol. 1991, 5:1273-1283.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1273-1283
    • Kontinen, V.P.1    Saris, P.2    Sarvas, M.3
  • 146
    • 84879840065 scopus 로고    scopus 로고
    • Developing Bacillus spp. as a cell factory for production of microbial enzymes and industrially important biochemicals in the context of systems and synthetic biology
    • Liu L., Liu Y., Shin H.D., Chen R.R., Wang N.S., Li J., Du G., Chen J. Developing Bacillus spp. as a cell factory for production of microbial enzymes and industrially important biochemicals in the context of systems and synthetic biology. Appl. Microbiol. Biotechnol. 2013, 97:6113-6127.
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 6113-6127
    • Liu, L.1    Liu, Y.2    Shin, H.D.3    Chen, R.R.4    Wang, N.S.5    Li, J.6    Du, G.7    Chen, J.8
  • 147
    • 84872192991 scopus 로고    scopus 로고
    • Getting the big beast to work - systems biotechnology of Bacillus megaterium for novel high-value proteins
    • Korneli C., David F., Biedendieck R., Jahn D., Wittmann C. Getting the big beast to work - systems biotechnology of Bacillus megaterium for novel high-value proteins. J. Biotechnol. 2013, 163:87-96.
    • (2013) J. Biotechnol. , vol.163 , pp. 87-96
    • Korneli, C.1    David, F.2    Biedendieck, R.3    Jahn, D.4    Wittmann, C.5
  • 148
    • 36249015337 scopus 로고    scopus 로고
    • A new Gateway (R) vector and expression protocol for fast and efficient recombinant protein expression in Mycobacterium smegmatis
    • Goldstone R.M., Moreland N.J., Bashiri G., Baker E.N., Lott J.S. A new Gateway (R) vector and expression protocol for fast and efficient recombinant protein expression in Mycobacterium smegmatis. Protein Expr. Purif. 2008, 57:81-87.
    • (2008) Protein Expr. Purif. , vol.57 , pp. 81-87
    • Goldstone, R.M.1    Moreland, N.J.2    Bashiri, G.3    Baker, E.N.4    Lott, J.S.5
  • 150
    • 1842578348 scopus 로고    scopus 로고
    • A novel system for expressing recombinant proteins over a wide temperature range from 4 to 35 degrees C
    • Nakashima N., Tamura T. A novel system for expressing recombinant proteins over a wide temperature range from 4 to 35 degrees C. Biotechnol. Bioeng. 2004, 86:136-148.
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 136-148
    • Nakashima, N.1    Tamura, T.2
  • 153
    • 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. 2013, 89:251-257.
    • (2013) Protein Expr. Purif. , vol.89 , pp. 251-257
    • An, S.J.1    Yim, S.S.2    Jeong, K.J.3
  • 154
    • 83555177335 scopus 로고    scopus 로고
    • Improving protein secretion of a transglutaminase-secreting Corynebacterium glutamicum recombinant strain on the basis of C-13 metabolic flux analysis
    • Umakoshi M., Hirasawa T., Furusawa C., Takenaka Y., Kikuchi Y., Shimizu H. Improving protein secretion of a transglutaminase-secreting Corynebacterium glutamicum recombinant strain on the basis of C-13 metabolic flux analysis. J. Biosci. Bioeng. 2011, 112:595-601.
    • (2011) J. Biosci. Bioeng. , vol.112 , pp. 595-601
    • Umakoshi, M.1    Hirasawa, T.2    Furusawa, C.3    Takenaka, Y.4    Kikuchi, Y.5    Shimizu, H.6
  • 155
    • 80052210447 scopus 로고    scopus 로고
    • Lactococci and lactobacilli as mucosal delivery vectors for therapeutic proteins and DNA vaccines
    • Bermudez-Humaran L.G., Kharrat P., Chatel J.M., Langella P. Lactococci and lactobacilli as mucosal delivery vectors for therapeutic proteins and DNA vaccines. Microb. Cell Fact. 2011, 10(Suppl 1):S4.
    • (2011) Microb. Cell Fact. , vol.10 , Issue.SUPPL. 1
    • Bermudez-Humaran, L.G.1    Kharrat, P.2    Chatel, J.M.3    Langella, P.4
  • 156
    • 0038796312 scopus 로고    scopus 로고
    • In situ delivery of therapeutic proteins by recombinant Lactococcus lactis
    • Steidler L., Neirynck S. In situ delivery of therapeutic proteins by recombinant Lactococcus lactis. J. Microbiol. 2003, 41:63-72.
    • (2003) J. Microbiol. , vol.41 , pp. 63-72
    • Steidler, L.1    Neirynck, S.2
  • 162
    • 84863641260 scopus 로고    scopus 로고
    • Clostridial spores for cancer therapy: targeting solid tumour microenvironment
    • Umer B., Good D., Anné J., Duan W., Wei M.Q. Clostridial spores for cancer therapy: targeting solid tumour microenvironment. J. Toxicol. 2012, 2012:8. 10.1155/2012/862764.
    • (2012) J. Toxicol. , vol.2012 , pp. 8
    • Umer, B.1    Good, D.2    Anné, J.3    Duan, W.4    Wei, M.Q.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.