메뉴 건너뛰기




Volumn 71, Issue 6, 2005, Pages 3085-3092

Increase in xylanase production by Streptomyces lividans through simultaneous use of the sec- and tat-dependent protein export systems

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; CATALYSIS; DISEASES; FLUORESCENCE; GENES;

EID: 20444408697     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.6.3085-3092.2005     Document Type: Article
Times cited : (18)

References (34)
  • 1
    • 0035812882 scopus 로고    scopus 로고
    • Export of Thermus thermophilus alkaline phosphatase via the twin-arginine translocation pathway in Escherichia coli
    • Angelini, S., R. Moreno, K. Gouffi, C.-L. Santini, A. Yamagishi, J. Berenger, and L.-F. Wu. 2001. Export of Thermus thermophilus alkaline phosphatase via the twin-arginine translocation pathway in Escherichia coli. FEBS Lett. 506:103-107.
    • (2001) FEBS Lett. , vol.506 , pp. 103-107
    • Angelini, S.1    Moreno, R.2    Gouffi, K.3    Santini, C.-L.4    Yamagishi, A.5    Berenger, J.6    Wu, L.-F.7
  • 2
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks, B. C. 1996. A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22:393-404.
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 4
    • 0030859180 scopus 로고    scopus 로고
    • Heterologous biopharmaceutical protein expression in Streptomyces
    • Binnie, C., J. D. Cossar, and D. I. Stewart. 1997. Heterologous biopharmaceutical protein expression in Streptomyces. Trends Biotechnol. 15:315-320.
    • (1997) Trends Biotechnol. , vol.15 , pp. 315-320
    • Binnie, C.1    Cossar, J.D.2    Stewart, D.I.3
  • 5
    • 6544229829 scopus 로고
    • A study on the conditions and mechanism of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid
    • Burton, K. 1956. A study on the conditions and mechanism of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid. Biochem. J. 62:315-323.
    • (1956) Biochem. J. , vol.62 , pp. 315-323
    • Burton, K.1
  • 6
    • 0029079118 scopus 로고
    • A new type of signal peptide: Central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase
    • Chaddock, A. M., A. Mant, I. Karnauchov, S. Brink, R. G. Herrmann, R. B. Klösgen, and C. Robinson. 1995. A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase. EMBO J. 14:2715-2722.
    • (1995) EMBO J. , vol.14 , pp. 2715-2722
    • Chaddock, A.M.1    Mant, A.2    Karnauchov, I.3    Brink, S.4    Herrmann, R.G.5    Klösgen, R.B.6    Robinson, C.7
  • 7
    • 0032432109 scopus 로고    scopus 로고
    • Targeting and assembly of periplasmic and outer membrane proteins in Escherichia coli
    • Danese, P. N., and T. J. Silhavy. 1998. Targeting and assembly of periplasmic and outer membrane proteins in Escherichia coli. Annu. Rev. Genet. 32:59-94.
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 59-94
    • Danese, P.N.1    Silhavy, T.J.2
  • 8
    • 0028070908 scopus 로고
    • Crystal structure, at 2.6-Å resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases
    • Derewenda, U., L. Swenson, R. Green, Y. Wei, R. Morosoli, F. Shareck, D. Kluepfel, and Z. S. Derewenda. 1994. Crystal structure, at 2.6-Å resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases. J. Biol. Chem. 269:20811-20814.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20811-20814
    • Derewenda, U.1    Swenson, L.2    Green, R.3    Wei, Y.4    Morosoli, R.5    Shareck, F.6    Kluepfel, D.7    Derewenda, Z.S.8
  • 9
    • 2542435943 scopus 로고    scopus 로고
    • Secretion of active xylanase C from Streptomyces lividans is exclusively mediated by the Tat protein export system
    • Faury, D., S. Saidane, H. Li, and R. Morosoli. 2004. Secretion of active xylanase C from Streptomyces lividans is exclusively mediated by the Tat protein export system. Biochim. Biophys. Acta 1699:155-162.
    • (2004) Biochim. Biophys. Acta , vol.1699 , pp. 155-162
    • Faury, D.1    Saidane, S.2    Li, H.3    Morosoli, R.4
  • 12
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R. M., H. D. Hunt, S. N. Ho, J. R. Pullen, and L. R. Pease. 1989. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77:61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.R.4    Pease, L.R.5
  • 13
    • 0029111794 scopus 로고
    • A cellulase/xylanase-negative mutant of Streptomyces lividans 1326 defective in cellobiose and xylobiose uptake is mutated in a gene encoding a protein homologous to ATP-binding proteins
    • Hurtubise, Y., F. Shareck, D. Kluepfel, and R. Morosoli. 1995. A cellulase/xylanase-negative mutant of Streptomyces lividans 1326 defective in cellobiose and xylobiose uptake is mutated in a gene encoding a protein homologous to ATP-binding proteins. Mol. Microbiol. 17:367-377.
    • (1995) Mol. Microbiol. , vol.17 , pp. 367-377
    • Hurtubise, Y.1    Shareck, F.2    Kluepfel, D.3    Morosoli, R.4
  • 14
    • 0002481409 scopus 로고
    • Enzymatic treatment of pulp
    • Jeffries, T. W. 1992. Enzymatic treatment of pulp. ACS Symp. Ser. 476:313-329.
    • (1992) ACS Symp. Ser. , vol.476 , pp. 313-329
    • Jeffries, T.W.1
  • 15
    • 0342264374 scopus 로고    scopus 로고
    • Increased xylanase production in Streptomyces lividans after replacement of the signal peptide: Dependence on box and inverted repeat sequence
    • Kébir, H., C. Dupont, and R. Morosoli. 2000. Increased xylanase production in Streptomyces lividans after replacement of the signal peptide: dependence on box and inverted repeat sequence. Biochim. Biophys. Acta 1491:177-184.
    • (2000) Biochim. Biophys. Acta , vol.1491 , pp. 177-184
    • Kébir, H.1    Dupont, C.2    Morosoli, R.3
  • 17
    • 0025270742 scopus 로고
    • Purification and characterization of a new xylanase (xylanase B) produced by Streptomyces lividans 66
    • Kluepfel, D., S. Vats-Mehta, F. Aumont, F. Shareck, and R. Morosoli. 1990. Purification and characterization of a new xylanase (xylanase B) produced by Streptomyces lividans 66. Biochem. J. 267:45-50.
    • (1990) Biochem. J. , vol.267 , pp. 45-50
    • Kluepfel, D.1    Vats-Mehta, S.2    Aumont, F.3    Shareck, F.4    Morosoli, R.5
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0022852923 scopus 로고
    • Purification and properties of a xylanase from Streptomyces lividans
    • Morosoli, R., J. L. Bertrand, F. Mondou, F. Shareck, and D. Kluepfel. 1986. Purification and properties of a xylanase from Streptomyces lividans. Biochem. J. 239:587-592.
    • (1986) Biochem. J. , vol.239 , pp. 587-592
    • Morosoli, R.1    Bertrand, J.L.2    Mondou, F.3    Shareck, F.4    Kluepfel, D.5
  • 20
    • 0032823550 scopus 로고    scopus 로고
    • Secretion of xylanase A2 in Streptomyces lividans: Dependence on signal peptides length, number and composition
    • Morosoli, R., and C. Dupont. 1999. Secretion of xylanase A2 in Streptomyces lividans: dependence on signal peptides length, number and composition. FEMS Microbiol. Lett. 179:437-445.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 437-445
    • Morosoli, R.1    Dupont, C.2
  • 21
    • 0030064497 scopus 로고    scopus 로고
    • Effect of signal peptide alterations and replacement on export of xylanase A in Streptomyces lividans
    • Pagé, N., D. Kluepfel, F. Shareck, and R. Morosoli. 1996. Effect of signal peptide alterations and replacement on export of xylanase A in Streptomyces lividans. Appl. Environ. Microbiol. 62:109-114.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 109-114
    • Pagé, N.1    Kluepfel, D.2    Shareck, F.3    Morosoli, R.4
  • 22
    • 0029924758 scopus 로고    scopus 로고
    • Increased xylanase yield in Streptomyces lividans: Dependence on number of ribosome-binding sites
    • Pagé, N., D. Kluepfel, F. Shareck, and R. Morosoli. 1996. Increased xylanase yield in Streptomyces lividans: dependence on number of ribosome-binding sites. Nat. Biotechnol. 14:756-759.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 756-759
    • Pagé, N.1    Kluepfel, D.2    Shareck, F.3    Morosoli, R.4
  • 23
    • 0035350689 scopus 로고    scopus 로고
    • Protein targeting by the twin-arginine translocation pathway
    • Robinson, C., and A. Bolhuis. 2001. Protein targeting by the twin-arginine translocation pathway. Nat. Rev. Mol. Cell Biol. 2:350-356.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 350-356
    • Robinson, C.1    Bolhuis, A.2
  • 24
    • 0027980013 scopus 로고
    • The presequence of a chimeric construct dictates which of two mechanisms are utilized for translocation across the thylakoid membrane: Evidence for the existence of two distinct translocation systems
    • Robinson, C., D. Cai, A. Hulford, I. W. Brock, D. Michl, L. Hazell, I. Schmidt, R. G. Herrmann, and R. B. Klösgen. 1994. The presequence of a chimeric construct dictates which of two mechanisms are utilized for translocation across the thylakoid membrane: evidence for the existence of two distinct translocation systems. EMBO J. 13:279-285.
    • (1994) EMBO J. , vol.13 , pp. 279-285
    • Robinson, C.1    Cai, D.2    Hulford, A.3    Brock, I.W.4    Michl, D.5    Hazell, L.6    Schmidt, I.7    Herrmann, R.G.8    Klösgen, R.B.9
  • 26
    • 0034944416 scopus 로고    scopus 로고
    • Transport of cytochrome c derivatives by the bacterial Tat protein translocation system
    • Sanders, C., N. Wethkamp, and H. Lill. 2001. Transport of cytochrome c derivatives by the bacterial Tat protein translocation system. Mol. Microbiol. 41:241-246.
    • (2001) Mol. Microbiol. , vol.41 , pp. 241-246
    • Sanders, C.1    Wethkamp, N.2    Lill, H.3
  • 28
    • 0032472381 scopus 로고    scopus 로고
    • A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini, C.-L., B. Ize, A. Chanal, M. Müller, G. Giordano, and L.-F. Wu. 1998. A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 17:101-112.
    • (1998) EMBO J. , vol.17 , pp. 101-112
    • Santini, C.-L.1    Ize, B.2    Chanal, A.3    Müller, M.4    Giordano, G.5    Wu, L.-F.6
  • 29
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of bacterial Sec-independent protein export pathway
    • Sargent, F., E. G. Bogsch, N. R. Stanley, M. Wexler, C. Robinson, B. C. Berks, and T. Palmer. 1998. Overlapping functions of components of bacterial Sec-independent protein export pathway. EMBO J. 17:3640-3650.
    • (1998) EMBO J. , vol.17 , pp. 3640-3650
    • Sargent, F.1    Bogsch, E.G.2    Stanley, N.R.3    Wexler, M.4    Robinson, C.5    Berks, B.C.6    Palmer, T.7
  • 30
    • 0026045488 scopus 로고
    • Sequences of three genes specifying xylanases in Streptomyces lividans
    • Shareck, F., C. Roy, M. Yaguchi, R. Morosoli, and D. Kluepfel. 1991. Sequences of three genes specifying xylanases in Streptomyces lividans. Gene 107:75-82.
    • (1991) Gene , vol.107 , pp. 75-82
    • Shareck, F.1    Roy, C.2    Yaguchi, M.3    Morosoli, R.4    Kluepfel, D.5
  • 31
    • 0034283706 scopus 로고    scopus 로고
    • Codon optimization of xylanase gene xynB from the thermophilic bacterium Dictyoglomus thermophilum for expression in the filamentous fungus Trichoderma reesei
    • Te'o, V. S., A. E. Cziferszky, P. L. Bergquist, and K. M. Nevalainen. 2000. Codon optimization of xylanase gene xynB from the thermophilic bacterium Dictyoglomus thermophilum for expression in the filamentous fungus Trichoderma reesei. FEMS Microbiol. Lett. 190:13-19.
    • (2000) FEMS Microbiol. Lett. , vol.190 , pp. 13-19
    • Te'o, V.S.1    Cziferszky, A.E.2    Bergquist, P.L.3    Nevalainen, K.M.4
  • 32
    • 0028911057 scopus 로고
    • Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei
    • Törronen, A., and J. Rouvinen. 1995. Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei. Biochemistry 34:847-856.
    • (1995) Biochemistry , vol.34 , pp. 847-856
    • Törronen, A.1    Rouvinen, J.2
  • 33
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.