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Volumn 127, Issue 2, 2007, Pages 211-221

Silent mutations at the 5′-end of the cDNA of actinoporins from the sea anemone Stichodactyla helianthus allow their heterologous overproduction in Escherichia coli

Author keywords

Actinoporin; Equinatoxin; Protein production; Ribosome binding site; Silent mutation; Sticholysin

Indexed keywords

DNA; ESCHERICHIA COLI; MUTAGENESIS; RNA; SPECTROSCOPIC ANALYSIS;

EID: 33846197988     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2006.07.006     Document Type: Article
Times cited : (36)

References (40)
  • 1
    • 4544352455 scopus 로고    scopus 로고
    • Phenotypic selection and characterization of randomly produced non-haemolytic mutants of the toxic sea anemone protein sticholysin II
    • Alegre-Cebollada J., Lacadena V., Oñaderra M., Mancheño J.M., Gavílanes J.G., and Martínez del Pozo A. Phenotypic selection and characterization of randomly produced non-haemolytic mutants of the toxic sea anemone protein sticholysin II. FEBS Lett. 575 (2004) 14-18
    • (2004) FEBS Lett. , vol.575 , pp. 14-18
    • Alegre-Cebollada, J.1    Lacadena, V.2    Oñaderra, M.3    Mancheño, J.M.4    Gavílanes, J.G.5    Martínez del Pozo, A.6
  • 2
    • 33644943981 scopus 로고    scopus 로고
    • Detergent-resistant membranes are platforms for actinoporin pore-forming activity on intact cells
    • Alegre-Cebollada J., Rodríguez-Crespo I., Gavilanes J.G., and Martínez del Pozo A. Detergent-resistant membranes are platforms for actinoporin pore-forming activity on intact cells. FEBS J. 273 (2006) 863-871
    • (2006) FEBS J. , vol.273 , pp. 863-871
    • Alegre-Cebollada, J.1    Rodríguez-Crespo, I.2    Gavilanes, J.G.3    Martínez del Pozo, A.4
  • 5
    • 0036027362 scopus 로고    scopus 로고
    • Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria)
    • Anderluh G., and Maček P. Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria). Toxicon 40 (2002) 111-124
    • (2002) Toxicon , vol.40 , pp. 111-124
    • Anderluh, G.1    Maček, P.2
  • 7
    • 0034880806 scopus 로고    scopus 로고
    • Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina
    • Athanasiadis A., Anderluh G., Maček P., and Turk D. Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina. Structure 9 (2001) 341-346
    • (2001) Structure , vol.9 , pp. 341-346
    • Athanasiadis, A.1    Anderluh, G.2    Maček, P.3    Turk, D.4
  • 8
    • 0032032911 scopus 로고    scopus 로고
    • Mechanism of the leakage induced on lipid model membranes by the hemolytic protein sticholysin II from the sea anemone Stichodactyla helianthus
    • de los Ríos V., Mancheño J.M., Lanio M.E., Oñaderra M., and Gavilanes J.G. Mechanism of the leakage induced on lipid model membranes by the hemolytic protein sticholysin II from the sea anemone Stichodactyla helianthus. Eur. J. Biochem. 252 (1998) 284-289
    • (1998) Eur. J. Biochem. , vol.252 , pp. 284-289
    • de los Ríos, V.1    Mancheño, J.M.2    Lanio, M.E.3    Oñaderra, M.4    Gavilanes, J.G.5
  • 11
    • 0025166089 scopus 로고
    • Secondary structure of the ribosome binding site determines translational efficiency: a quantitative analysis
    • de Smit M.H., and Van Duin J. Secondary structure of the ribosome binding site determines translational efficiency: a quantitative analysis. Proc. Natl. Acad. Sci. U.S.A. 87 (1990) 7668-7772
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 7668-7772
    • de Smit, M.H.1    Van Duin, J.2
  • 13
    • 0021890825 scopus 로고
    • 2+-induced fusion and destabilization of liposomes
    • 2+-induced fusion and destabilization of liposomes. Biochemistry 24 (1985) 3099-3106
    • (1985) Biochemistry , vol.24 , pp. 3099-3106
    • Ellens, H.1    Bentz, J.2    Szoka, F.C.3
  • 14
    • 0036304122 scopus 로고    scopus 로고
    • Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II: implications for pore formation
    • Hinds M.G., Zhang W., Anderluh G., Hansen P.E., and Norton R.S. Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II: implications for pore formation. J. Mol. Biol. 315 (2002) 1219-1229
    • (2002) J. Mol. Biol. , vol.315 , pp. 1219-1229
    • Hinds, M.G.1    Zhang, W.2    Anderluh, G.3    Hansen, P.E.4    Norton, R.S.5
  • 15
    • 0043123153 scopus 로고    scopus 로고
    • Vienna RNA secondary structure server
    • Hofacker I.L. Vienna RNA secondary structure server. Nucleic Acid Res. 31 (2003) 3429-3431
    • (2003) Nucleic Acid Res. , vol.31 , pp. 3429-3431
    • Hofacker, I.L.1
  • 17
    • 0142121656 scopus 로고    scopus 로고
    • High-level expression of porcine liver cytochrome P-450 reductase catalytic domain in Escherichia coli by modulating the predicted local secondary structure of mRNA
    • Kimura S., and lyanagi T. High-level expression of porcine liver cytochrome P-450 reductase catalytic domain in Escherichia coli by modulating the predicted local secondary structure of mRNA. J. Biochem. (Tokyo) 134 (2003) 403-413
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 403-413
    • Kimura, S.1    lyanagi, T.2
  • 18
    • 0033061571 scopus 로고    scopus 로고
    • Initiation of translation in prokaryotes and eukaryotes
    • Kozak M. Initiation of translation in prokaryotes and eukaryotes. Gene 234 (1999) 187-208
    • (1999) Gene , vol.234 , pp. 187-208
    • Kozak, M.1
  • 21
    • 0344099389 scopus 로고    scopus 로고
    • Expression and purification of SrcI from sea anemone Sagartia rosea as a recombinant non-fusion protein
    • Jiang X., Peng L., Yang W., Tang X., Liu W., and Xu A. Expression and purification of SrcI from sea anemone Sagartia rosea as a recombinant non-fusion protein. Prot. Exp. Purif. 32 (2003) 161-166
    • (2003) Prot. Exp. Purif. , vol.32 , pp. 161-166
    • Jiang, X.1    Peng, L.2    Yang, W.3    Tang, X.4    Liu, W.5    Xu, A.6
  • 23
    • 0023046899 scopus 로고
    • Secondary structure as primary determinant of the efficiency of ribosomal binding sites in Escherichia coli
    • Looman A.C., Bodlaender J., de Gruyter M., Vogelaar A., and Van Knippenberg P.H. Secondary structure as primary determinant of the efficiency of ribosomal binding sites in Escherichia coli. Nucleic Aic Res. 14 (1986) 5481-5497
    • (1986) Nucleic Aic Res. , vol.14 , pp. 5481-5497
    • Looman, A.C.1    Bodlaender, J.2    de Gruyter, M.3    Vogelaar, A.4    Van Knippenberg, P.H.5
  • 24
    • 0028351423 scopus 로고
    • Mechanism of action of equinatoxin II, a cytolysin from the sea anemone Actinia equina L. belonging to the family of actinoporins
    • Maček P., Belmonte G., Pederzolli C., and Menestrina G. Mechanism of action of equinatoxin II, a cytolysin from the sea anemone Actinia equina L. belonging to the family of actinoporins. Toxicology 87 (1994) 205-221
    • (1994) Toxicology , vol.87 , pp. 205-221
    • Maček, P.1    Belmonte, G.2    Pederzolli, C.3    Menestrina, G.4
  • 25
    • 0026784112 scopus 로고
    • Polypeptide cytolytic toxins from sea anemones (Actinaria)
    • Maček P. Polypeptide cytolytic toxins from sea anemones (Actinaria). FEMS Microbiol. Immunol. 105 (1992) 121-129
    • (1992) FEMS Microbiol. Immunol. , vol.105 , pp. 121-129
    • Maček, P.1
  • 26
  • 28
    • 0242542032 scopus 로고    scopus 로고
    • Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation
    • Mancheño J.M., Martín-Benito J., Martínez-Ripoll M., Gavilanes J.G., and Hermoso J.A. Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation. Structure 11 (2003) 1319-1328
    • (2003) Structure , vol.11 , pp. 1319-1328
    • Mancheño, J.M.1    Martín-Benito, J.2    Martínez-Ripoll, M.3    Gavilanes, J.G.4    Hermoso, J.A.5
  • 30
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews D.H., Sabina J., Zuker M., and Turner D.H. Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J. Mol. Biol. 288 (1999) 911-940
    • (1999) J. Mol. Biol. , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 31
    • 9244241054 scopus 로고    scopus 로고
    • Pore-forming toxins: from structure to function
    • Parker M.W., and Feil S.C. Pore-forming toxins: from structure to function. Progr. Biophys. Mol. Biol. 88 (2005) 91-142
    • (2005) Progr. Biophys. Mol. Biol. , vol.88 , pp. 91-142
    • Parker, M.W.1    Feil, S.C.2
  • 32
    • 3042632236 scopus 로고    scopus 로고
    • RNA stem-loop enhanced expression of previously non-expressible genes
    • Paulus M., Haslbeck M., and Watzele M. RNA stem-loop enhanced expression of previously non-expressible genes. Nucleic Acid Res. 32 9 (2004) e78
    • (2004) Nucleic Acid Res. , vol.32 , Issue.9
    • Paulus, M.1    Haslbeck, M.2    Watzele, M.3
  • 33
    • 0242289562 scopus 로고    scopus 로고
    • Comparison of pore-forming ability in membranes of a native and a recombinant variant of Sticholysin II from Stichodactyla helianthus
    • Pazos I.F., Martínez D., Tejuca M., Valle A., del Pozo A., Álvarez C., Lanio M.E., and Lissi E.A. Comparison of pore-forming ability in membranes of a native and a recombinant variant of Sticholysin II from Stichodactyla helianthus. Toxicon 42 (2003) 571-578
    • (2003) Toxicon , vol.42 , pp. 571-578
    • Pazos, I.F.1    Martínez, D.2    Tejuca, M.3    Valle, A.4    del Pozo, A.5    Álvarez, C.6    Lanio, M.E.7    Lissi, E.A.8
  • 36
    • 33645965566 scopus 로고    scopus 로고
    • Unfolding of mRNA secondary structure by the bacterial translation initiation complex
    • Studer S.M., and Joseph S. Unfolding of mRNA secondary structure by the bacterial translation initiation complex. Mol. Cell 22 (2006) 105-115
    • (2006) Mol. Cell , vol.22 , pp. 105-115
    • Studer, S.M.1    Joseph, S.2
  • 37
    • 0026338431 scopus 로고
    • Cytolytic toxins from sea anemones
    • Turk T. Cytolytic toxins from sea anemones. J. Toxicol. Toxin Rev. 10 (1991) 223-262
    • (1991) J. Toxicol. Toxin Rev. , vol.10 , pp. 223-262
    • Turk, T.1
  • 38
    • 14844320117 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of hemolysin from the sea anemone Actineria villosa
    • Uechi G., Toma H., Arakawa T., and Sato Y. Molecular cloning and functional expression of hemolysin from the sea anemone Actineria villosa. Prot. Exp. Purif. 40 (2005) 379-384
    • (2005) Prot. Exp. Purif. , vol.40 , pp. 379-384
    • Uechi, G.1    Toma, H.2    Arakawa, T.3    Sato, Y.4
  • 39
    • 0034673740 scopus 로고    scopus 로고
    • A new cytolysin from the sea anemone, Heteractis magnifica: Isolation, cDNA cloning and functional expression
    • Wang Y., Chua K.L., and Khoo H.E. A new cytolysin from the sea anemone, Heteractis magnifica: Isolation, cDNA cloning and functional expression. Biochim. Biophys. Acta 1478 (2000) 9-18
    • (2000) Biochim. Biophys. Acta , vol.1478 , pp. 9-18
    • Wang, Y.1    Chua, K.L.2    Khoo, H.E.3
  • 40
    • 0026574167 scopus 로고
    • Importance of mRNA folding and start codon accessibility in the expression of genes in a ribosomal protein operon of Escherichi coli
    • Wikstrom P.M., Lind L.K., Berg D.E., and Bjork G.R. Importance of mRNA folding and start codon accessibility in the expression of genes in a ribosomal protein operon of Escherichi coli. J. Mol. Biol. 224 (1992) 949-966
    • (1992) J. Mol. Biol. , vol.224 , pp. 949-966
    • Wikstrom, P.M.1    Lind, L.K.2    Berg, D.E.3    Bjork, G.R.4


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