메뉴 건너뛰기




Volumn 16, Issue 1, 2017, Pages

Cell surface engineering of Bacillus subtilis improves production yields of heterologously expressed α-amylases

Author keywords

Bacillus; Cardiolipin; ClsA; Electrostatic interaction; Phosphatidylglycerol; Protein secretion; PssA; Amylases

Indexed keywords

AMYLASE; CARDIOLIPIN; MEMBRANE PHOSPHOLIPID; PHOSPHATIDYLGLYCEROL;

EID: 85016934159     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/s12934-017-0674-0     Document Type: Article
Times cited : (23)

References (37)
  • 1
    • 0026752273 scopus 로고
    • Bacillus subtilis and its relatives: molecular biological and industrial workhorses
    • Harwood CR. Bacillus subtilis and its relatives: molecular biological and industrial workhorses. Trends Biotechnol. 1992;10:247-56.
    • (1992) Trends Biotechnol , vol.10 , pp. 247-256
    • Harwood, C.R.1
  • 2
    • 39049125071 scopus 로고    scopus 로고
    • Bacillus protein secretion: an unfolding story
    • Harwood CR, Cranenburgh R. Bacillus protein secretion: an unfolding story. Trends Microbiol. 2008;16:73-9.
    • (2008) Trends Microbiol , vol.16 , pp. 73-79
    • Harwood, C.R.1    Cranenburgh, R.2
  • 3
    • 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 WJ. Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism. Biochim Biophys Acta. 2004;1694:299-310.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 299-310
    • Westers, L.1    Westers, H.2    Quax, W.J.3
  • 4
    • 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
  • 5
    • 48049110998 scopus 로고    scopus 로고
    • Enhanced recombinant protein productivity by genome reduction in Bacillus subtilis
    • Morimoto T, Kadoya R, Endo K, Tohata M, Sawada K, Liu S. Enhanced recombinant protein productivity by genome reduction in Bacillus subtilis. DNA Res. 2008;15:73-81.
    • (2008) DNA Res , vol.15 , pp. 73-81
    • Morimoto, T.1    Kadoya, R.2    Endo, K.3    Tohata, M.4    Sawada, K.5    Liu, S.6
  • 6
    • 33845946823 scopus 로고    scopus 로고
    • Protein secretion pathways in Bacillus subtilis: implication for optimization of heterologous protein secretion
    • Fu LL, Xu ZR, Li WF, Shuai JB, Lu P, Hu CX. Protein secretion pathways in Bacillus subtilis: implication for optimization of heterologous protein secretion. Biotechnol Adv. 2007;25:1-12.
    • (2007) Biotechnol Adv , vol.25 , pp. 1-12
    • Fu, L.L.1    Xu, Z.R.2    Li, W.F.3    Shuai, J.B.4    Lu, P.5    Hu, C.X.6
  • 7
    • 55849145907 scopus 로고    scopus 로고
    • Optimization of protein secretion by Bacillus subtilis
    • Nijland R, Kuipers OP. Optimization of protein secretion by Bacillus subtilis. Recent Pat Biotechnol. 2008;2:79-87.
    • (2008) Recent Pat Biotechnol , vol.2 , pp. 79-87
    • Nijland, R.1    Kuipers, O.P.2
  • 8
    • 77956107104 scopus 로고    scopus 로고
    • Heterologous protein secretion by Bacillus species: from the cradle to the grave
    • Pohl S, Harwood CR. Heterologous protein secretion by Bacillus species: from the cradle to the grave. Adv Appl Microbiol. 2010;73:1-25.
    • (2010) Adv Appl Microbiol , vol.73 , pp. 1-25
    • Pohl, S.1    Harwood, C.R.2
  • 9
    • 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
    • Kakeshita 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;46:250-7.
    • (2010) Mol Biotechnol , vol.46 , pp. 250-257
    • Kakeshita, H.1    Kageyama, Y.2    Ara, K.3    Ozaki, K.4    Nakamura, K.5
  • 10
    • 23044435305 scopus 로고    scopus 로고
    • Secretion of heterologous proteins in Bacillus subtilis can be improved by engineering cell components affecting post-translocational protein folding and degradation
    • Vitikainen M, Hyyrylainen HL, Kivimaki A, Kontinen VP, Sarvas M. Secretion of heterologous proteins in Bacillus subtilis can be improved by engineering cell components affecting post-translocational protein folding and degradation. J Appl Microbiol. 2005;99:363-75.
    • (2005) J Appl Microbiol , vol.99 , pp. 363-375
    • Vitikainen, M.1    Hyyrylainen, H.L.2    Kivimaki, A.3    Kontinen, V.P.4    Sarvas, M.5
  • 11
    • 0036135303 scopus 로고    scopus 로고
    • Optimization of the cell wall microenvironment allows increased production of recombinant Bacillus anthracis protective antigen from B. subtilis
    • Thwaite JE, Baillie LWJ, Carter NM, Stephenson K, Rees M, Harwood CR, et al. Optimization of the cell wall microenvironment allows increased production of recombinant Bacillus anthracis protective antigen from B. subtilis. Appl Environ Microbiol. 2002;68:227-34.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 227-234
    • Thwaite, J.E.1    Baillie, L.W.J.2    Carter, N.M.3    Stephenson, K.4    Rees, M.5    Harwood, C.R.6
  • 12
    • 78049311718 scopus 로고    scopus 로고
    • Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and heterologous signal peptides
    • Degering C, Eggert T, Puls M, Bongaerts J, Evers S, Maurer KH, et al. Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and heterologous signal peptides. Appl Environ Microbiol. 2010;76:6370-6.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 6370-6376
    • Degering, C.1    Eggert, T.2    Puls, M.3    Bongaerts, J.4    Evers, S.5    Maurer, K.H.6
  • 13
    • 33645099878 scopus 로고    scopus 로고
    • Role of anionic phospholipids in the adaptation of Bacillus subtilis to high salinity
    • Lopez CS, Alice AF, Heras H, Rivas EA, Sanchez-Rivas C. Role of anionic phospholipids in the adaptation of Bacillus subtilis to high salinity. Microbiology. 2006;152:605-16.
    • (2006) Microbiology , vol.152 , pp. 605-616
    • Lopez, C.S.1    Alice, A.F.2    Heras, H.3    Rivas, E.A.4    Sanchez-Rivas, C.5
  • 14
    • 0347469684 scopus 로고    scopus 로고
    • Variations of the envelope composition of Bacillus subtilis during growth in hyperosmotic medium
    • Lopez CS, Heras H, Ruzal SM, Sanchez-Rivas C, Rivas EA. Variations of the envelope composition of Bacillus subtilis during growth in hyperosmotic medium. Curr Microbiol. 1998;36:55-61.
    • (1998) Curr Microbiol , vol.36 , pp. 55-61
    • Lopez, C.S.1    Heras, H.2    Ruzal, S.M.3    Sanchez-Rivas, C.4    Rivas, E.A.5
  • 17
    • 0033407138 scopus 로고    scopus 로고
    • Requirement for phospholipids of the translocation of the trimethylamine n-oxide reductase through the Tat pathway in Escherichia coli
    • Mikhaleva NI, Santini CL, Giordano G, Nesmeyanova MA, Wu LF. Requirement for phospholipids of the translocation of the trimethylamine n-oxide reductase through the Tat pathway in Escherichia coli. FEBS Lett. 1999;463:331-5.
    • (1999) FEBS Lett , vol.463 , pp. 331-335
    • Mikhaleva, N.I.1    Santini, C.L.2    Giordano, G.3    Nesmeyanova, M.A.4    Wu, L.F.5
  • 18
    • 0034282698 scopus 로고    scopus 로고
    • d-Alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis
    • Hyyrylainen HL, Vitikainen M, Thwaite J, Wu H, Sarvas M, Harwood CR, et al. d-Alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis. J Biol Chem. 2000;275:26696-703.
    • (2000) J Biol Chem , vol.275 , pp. 26696-26703
    • Hyyrylainen, H.L.1    Vitikainen, M.2    Thwaite, J.3    Wu, H.4    Sarvas, M.5    Harwood, C.R.6
  • 19
    • 0028173341 scopus 로고
    • Molecular structures of penicillin-binding proteins and β-lactamases
    • Ghuysen JM. Molecular structures of penicillin-binding proteins and β-lactamases. Trends Microbiol. 1994;2:372-80.
    • (1994) Trends Microbiol , vol.2 , pp. 372-380
    • Ghuysen, J.M.1
  • 20
    • 0032985757 scopus 로고    scopus 로고
    • Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation
    • Atrih A, Bacher G, Allmaier G, Williamson MP, Foster SJ. Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation. J Bacteriol. 1999;181:3956-66.
    • (1999) J Bacteriol , vol.181 , pp. 3956-3966
    • Atrih, A.1    Bacher, G.2    Allmaier, G.3    Williamson, M.P.4    Foster, S.J.5
  • 21
    • 0034663718 scopus 로고    scopus 로고
    • The influence of secretory-protein charge on late stages of secretion from the Gram-positive bacterium Bacillus subtilis
    • Stephenson K, Jensen CL, Jorgensen ST, Lakey JH, Harwood CR. The influence of secretory-protein charge on late stages of secretion from the Gram-positive bacterium Bacillus subtilis. Biochem J. 2000;350:31-9.
    • (2000) Biochem J , vol.350 , pp. 31-39
    • Stephenson, K.1    Jensen, C.L.2    Jorgensen, S.T.3    Lakey, J.H.4    Harwood, C.R.5
  • 22
    • 57349161246 scopus 로고    scopus 로고
    • Phenotypic and transcriptomic characterization of Bacillus subtilis mutants with grossly altered membrane composition
    • Salzberg LI, Helmann JD. Phenotypic and transcriptomic characterization of Bacillus subtilis mutants with grossly altered membrane composition. J Bacteriol. 2008;190:7797-807.
    • (2008) J Bacteriol , vol.190 , pp. 7797-7807
    • Salzberg, L.I.1    Helmann, J.D.2
  • 26
    • 0021193861 scopus 로고
    • Construction of a Bacillus subtilis double mutant deficient in extracellular alkaline and neutral proteases
    • Kawamura F, Doi RH. Construction of a Bacillus subtilis double mutant deficient in extracellular alkaline and neutral proteases. J Bacteriol. 1984;160:442-4.
    • (1984) J Bacteriol , vol.160 , pp. 442-444
    • Kawamura, F.1    Doi, R.H.2
  • 28
    • 85019863247 scopus 로고    scopus 로고
    • Cell surface and membrane engineering: emerging technologies and applications
    • Saeui CT, Mathew MP, Liu L, Urias E, Yarema KJ. Cell surface and membrane engineering: emerging technologies and applications. Funct Biomater. 2015;6:454-85.
    • (2015) Funct Biomater , vol.6 , pp. 454-485
    • Saeui, C.T.1    Mathew, M.P.2    Liu, L.3    Urias, E.4    Yarema, K.J.5
  • 29
    • 84976468234 scopus 로고    scopus 로고
    • Establishment of cell surface engineering and its development
    • Ueda M. Establishment of cell surface engineering and its development. Biosci Biotechnol Biochem. 2016;80:1243-53.
    • (2016) Biosci Biotechnol Biochem , vol.80 , pp. 1243-1253
    • Ueda, M.1
  • 30
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos C, Spizizen J. Requirements for transformation in Bacillus subtilis. J Bacteriol. 1961;81:741-6.
    • (1961) J Bacteriol , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 31
    • 29144508806 scopus 로고    scopus 로고
    • Development and characterization of a subtilin-regulated expression system in Bacillus subtilis: strict control of gene expression by addition of subtilin
    • Bongers RS, Veening JW, Van Wieringen M, Kuipers OP, Kleerebezem M. Development and characterization of a subtilin-regulated expression system in Bacillus subtilis: strict control of gene expression by addition of subtilin. Appl Environ Microbiol. 2005;71:8818-24.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8818-8824
    • Bongers, R.S.1    Veening, J.W.2    Wieringen, M.3    Kuipers, O.P.4    Kleerebezem, M.5
  • 33
    • 77950603940 scopus 로고    scopus 로고
    • A mutant Pfu DNA polymerase designed for advanced uracil-excision DNA engineering
    • Norholm MH. A mutant Pfu DNA polymerase designed for advanced uracil-excision DNA engineering. BMC Biotechnol. 2010;10:21.
    • (2010) BMC Biotechnol , vol.10 , pp. 21
    • Norholm, M.H.1
  • 35
    • 0347320637 scopus 로고    scopus 로고
    • Osmotic response in Lactobacillus casei ATCC 393: biochemical and biophysical characteristics of membrane
    • Machado MC, Lopez CS, Heras H, Rivas EA. Osmotic response in Lactobacillus casei ATCC 393: biochemical and biophysical characteristics of membrane. Arch Biochem Biophys. 2004;422:61-70.
    • (2004) Arch Biochem Biophys , vol.422 , pp. 61-70
    • Machado, M.C.1    Lopez, C.S.2    Heras, H.3    Rivas, E.A.4
  • 36
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban MJ, Cohen SN. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J Mol Biol. 1980;138:179-207.
    • (1980) J Mol Biol , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 37
    • 0025809486 scopus 로고
    • New pUC-derived cloning vectors with different selectable markers and DNA replication origins
    • Vieira J, Messing J. New pUC-derived cloning vectors with different selectable markers and DNA replication origins. Gene. 1991;100:189-94.
    • (1991) Gene , vol.100 , pp. 189-194
    • Vieira, J.1    Messing, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.