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Volumn 390, Issue 3, 2009, Pages 673-677

Overexpression of IbpB enhances production of soluble active Streptomyces olivaceovirdis XynB in Escherichia coli

Author keywords

IbpB; Streptomyces olivaceovirdis; XynB

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 100; HEAT SHOCK PROTEIN 70; PROTEIN IBPB; PROTEIN XYNB; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 70449697874     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.10.026     Document Type: Article
Times cited : (3)

References (13)
  • 1
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee G.J., Roseman A.M., Saibil H.R., and Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16 (1997) 659-671
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 2
    • 0032079487 scopus 로고    scopus 로고
    • The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • Veinger L., Diamant S., Buchner J., and Goloubinoff P. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J. Biol. Chem. 273 (1998) 11032-11037
    • (1998) J. Biol. Chem. , vol.273 , pp. 11032-11037
    • Veinger, L.1    Diamant, S.2    Buchner, J.3    Goloubinoff, P.4
  • 3
    • 0026726710 scopus 로고
    • Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli
    • Lee S.C., and Olins P.O. Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli. J. Biol. Chem. 267 (1992) 2849-2852
    • (1992) J. Biol. Chem. , vol.267 , pp. 2849-2852
    • Lee, S.C.1    Olins, P.O.2
  • 4
    • 0028850389 scopus 로고
    • Human protein disulfide isomerase functionally complements a dsba mutation and enhances the yield of pectate lyase C in Escherichia coli
    • Humphreys D.P., Weir N., Mountain A., and Lund P.A. Human protein disulfide isomerase functionally complements a dsba mutation and enhances the yield of pectate lyase C in Escherichia coli. J. Biol. Chem. 270 (1995) 28210-28215
    • (1995) J. Biol. Chem. , vol.270 , pp. 28210-28215
    • Humphreys, D.P.1    Weir, N.2    Mountain, A.3    Lund, P.A.4
  • 5
    • 15844371986 scopus 로고    scopus 로고
    • Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds
    • Ostermeier M., De Sutter K., and Georgiou G. Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds. J. Biol. Chem. 271 (1996) 10616-10622
    • (1996) J. Biol. Chem. , vol.271 , pp. 10616-10622
    • Ostermeier, M.1    De Sutter, K.2    Georgiou, G.3
  • 6
    • 53349107463 scopus 로고    scopus 로고
    • Microbial small heat shock proteins and their use in biotechnology
    • Han M.J., Yun H., and Lee S.Y. Microbial small heat shock proteins and their use in biotechnology. Biotechnol. Adv. 26 (2008) 591-609
    • (2008) Biotechnol. Adv. , vol.26 , pp. 591-609
    • Han, M.J.1    Yun, H.2    Lee, S.Y.3
  • 7
    • 58549098512 scopus 로고    scopus 로고
    • Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation
    • Ratajczak E., Zie{ogonek}tkiewicz S., and Liberek K. Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation. J. Mol. Biol. 386 (2009) 178-189
    • (2009) J. Mol. Biol. , vol.386 , pp. 178-189
    • Ratajczak, E.1    Zietkiewicz, S.2    Liberek, K.3
  • 8
    • 23244464653 scopus 로고    scopus 로고
    • The small heat-shock proteins IbpA and IbpB reduce the stress load of recombinant Escherichia coli and delay degradation of inclusion bodies
    • LeThanh H., Neubauer P., and Hoffmann F. The small heat-shock proteins IbpA and IbpB reduce the stress load of recombinant Escherichia coli and delay degradation of inclusion bodies. Microb. Cell Fact 4 (2005) 6
    • (2005) Microb. Cell Fact , vol.4 , pp. 6
    • LeThanh, H.1    Neubauer, P.2    Hoffmann, F.3
  • 10
    • 28644445655 scopus 로고    scopus 로고
    • A two-dimensional electrophoresis proteomic reference map and systematic identification of 1367 proteins from a cell suspension culture of the model legume Medicago truncatula
    • Lei Z., Elmer A.M., Watson B.S., Dixon R.A., Mendes P.J., and Sumner L.W. A two-dimensional electrophoresis proteomic reference map and systematic identification of 1367 proteins from a cell suspension culture of the model legume Medicago truncatula. Mol. Cell. Proteomics 4 (2005) 1812-1825
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1812-1825
    • Lei, Z.1    Elmer, A.M.2    Watson, B.S.3    Dixon, R.A.4    Mendes, P.J.5    Sumner, L.W.6
  • 11
    • 0030877168 scopus 로고    scopus 로고
    • Mutation of a highly conserved arginine in motif IV of Escherichia coli DNA helicase II results in an ATP-binding defect
    • Hall M.C., and Matson S.W. Mutation of a highly conserved arginine in motif IV of Escherichia coli DNA helicase II results in an ATP-binding defect. J. Biol. Chem. 272 (1997) 18614-18620
    • (1997) J. Biol. Chem. , vol.272 , pp. 18614-18620
    • Hall, M.C.1    Matson, S.W.2
  • 12
    • 14844355848 scopus 로고    scopus 로고
    • The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli
    • Jiao W., Qian M., Li P., and Chang Z. The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli. J. Mol. Biol. 347 (2005) 871-884
    • (2005) J. Mol. Biol. , vol.347 , pp. 871-884
    • Jiao, W.1    Qian, M.2    Li, P.3    Chang, Z.4
  • 13
    • 0028819842 scopus 로고
    • Effects of overexpressing folding modulators on the in vivo folding of heterologous proteins in Escherichia coli
    • Wall J.G., and Plückthun A. Effects of overexpressing folding modulators on the in vivo folding of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6 (1995) 507-516
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 507-516
    • Wall, J.G.1    Plückthun, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.