메뉴 건너뛰기




Volumn 101, Issue 5, 2008, Pages 967-974

Silent mutations result in HlyA hypersecretion by reducing intracellular HlyA protein aggregates

Author keywords

hemolysin; Hemolysin pathway; Rare codon; Type I

Indexed keywords

AGGLOMERATION; BLOOD; ENZYME ACTIVITY; ESCHERICHIA COLI; PROTEINS; TRANSLATION (LANGUAGES);

EID: 56449096169     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.21979     Document Type: Article
Times cited : (11)

References (27)
  • 1
    • 0028533504 scopus 로고
    • Heterologous protein secretion and the versatile Escherichia coli haemolysin translocator
    • Blight MA, Holland IB. 1994. Heterologous protein secretion and the versatile Escherichia coli haemolysin translocator. Trend Biotechnol 12:450-455.
    • (1994) Trend Biotechnol , vol.12 , pp. 450-455
    • Blight, M.A.1    Holland, I.B.2
  • 3
    • 0022254465 scopus 로고
    • Escherichia coli hemolysin is released extracellularly without cleavage of a signal peptide
    • Felmlee T, Pellett S, Lee EY, Welch RA. 1985a. Escherichia coli hemolysin is released extracellularly without cleavage of a signal peptide. J Bacteriol 163:88-93.
    • (1985) J Bacteriol , vol.163 , pp. 88-93
    • Felmlee, T.1    Pellett, S.2    Lee, E.Y.3    Welch, R.A.4
  • 4
    • 0022260426 scopus 로고
    • Nucleotide sequence of an Escherichia coli chromosomal hemolysin
    • Felmlee T, Pellett S, Welch RA. 1985b. Nucleotide sequence of an Escherichia coli chromosomal hemolysin. J Bacteriol 163:94-105.
    • (1985) J Bacteriol , vol.163 , pp. 94-105
    • Felmlee, T.1    Pellett, S.2    Welch, R.A.3
  • 5
    • 0024041944 scopus 로고
    • Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion
    • Felmlee T, Welch RA. 1988. Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion. Proc Natl Acad Sci USA 85:5269-5273.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5269-5273
    • Felmlee, T.1    Welch, R.A.2
  • 6
    • 0022981351 scopus 로고
    • Localization of inclusion bodies in Escherichia coli overproducing beta-lactamase or alkaline phosphatase
    • Georgiou G, Telford JN, Shuler ML, Wilson DB. 1986. Localization of inclusion bodies in Escherichia coli overproducing beta-lactamase or alkaline phosphatase. Appl Environ Microbiol 52:1157-1161.
    • (1986) Appl Environ Microbiol , vol.52 , pp. 1157-1161
    • Georgiou, G.1    Telford, J.N.2    Shuler, M.L.3    Wilson, D.B.4
  • 7
    • 0019474499 scopus 로고
    • Correlation between the abundance of E. coli transfer RNAs and the occurrence of the respective codon in the protein genes
    • Ikemura T. 1981. Correlation between the abundance of E. coli transfer RNAs and the occurrence of the respective codon in the protein genes. J Mol Biol 146:1-21.
    • (1981) J Mol Biol , vol.146 , pp. 1-21
    • Ikemura, T.1
  • 9
    • 0032699491 scopus 로고    scopus 로고
    • Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation
    • Komar AA, Lesnik T, Reiss C. 1999. Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation. FEBS Lett 462:387-391.
    • (1999) FEBS Lett , vol.462 , pp. 387-391
    • Komar, A.A.1    Lesnik, T.2    Reiss, C.3
  • 10
    • 12544253743 scopus 로고    scopus 로고
    • Engineering HlyA hypersecretion in Escherichia coli based on proteomic and microarray analyses
    • Lee PS, Lee KH. 2005. Engineering HlyA hypersecretion in Escherichia coli based on proteomic and microarray analyses. Biotechnol Bioeng 89:195-205.
    • (2005) Biotechnol Bioeng , vol.89 , pp. 195-205
    • Lee, P.S.1    Lee, K.H.2
  • 11
    • 0036412057 scopus 로고    scopus 로고
    • Cloning and hemolysin mediated secretory expression of a codon-optimized synthetic human interleukin-6 gene in Escherichia coli
    • Li YY, Chen CX, von Specht BU, Hahn HP. 2002. Cloning and hemolysin mediated secretory expression of a codon-optimized synthetic human interleukin-6 gene in Escherichia coli. Protein Expr Purif 25:437-447.
    • (2002) Protein Expr Purif , vol.25 , pp. 437-447
    • Li, Y.Y.1    Chen, C.X.2    von Specht, B.U.3    Hahn, H.P.4
  • 12
    • 0034708415 scopus 로고    scopus 로고
    • Folding of a synthetic parallel beta-roll protein
    • Lilie H, Haehnel W, Rudolph R, Baumann U. 2000. Folding of a synthetic parallel beta-roll protein. FEBS Lett 470:173-177.
    • (2000) FEBS Lett , vol.470 , pp. 173-177
    • Lilie, H.1    Haehnel, W.2    Rudolph, R.3    Baumann, U.4
  • 14
    • 0033020320 scopus 로고    scopus 로고
    • Antibody analysis of the localisation, expression and stability of HlyD, the MFP component of the E. coli haemolysin translocator
    • Pimenta AL, Young J, Holland IB, Blight MA. 1999. Antibody analysis of the localisation, expression and stability of HlyD, the MFP component of the E. coli haemolysin translocator. Mol Gen Genet 261:122-132.
    • (1999) Mol Gen Genet , vol.261 , pp. 122-132
    • Pimenta, A.L.1    Young, J.2    Holland, I.B.3    Blight, M.A.4
  • 15
    • 56449123499 scopus 로고    scopus 로고
    • Totally asymmetric exclusion process with extended objects: A model for protein synthesis. Phys Rev E
    • 1-17
    • Shaw L, Zia R, Lee KH. 2003. Totally asymmetric exclusion process with extended objects: A model for protein synthesis. Phys Rev E 68:021910(1-17).
    • (2003) , vol.68 , pp. 021910
    • Shaw, L.1    Zia, R.2    Lee, K.H.3
  • 16
    • 9244231763 scopus 로고    scopus 로고
    • Translational level is a critical factor for the secretion of heterologous proteins in Escherichia coli
    • Simmons LC, Yansura DG. 1996. Translational level is a critical factor for the secretion of heterologous proteins in Escherichia coli. Nat Biotechnol 14:629-634.
    • (1996) Nat Biotechnol , vol.14 , pp. 629-634
    • Simmons, L.C.1    Yansura, D.G.2
  • 17
    • 0031582214 scopus 로고    scopus 로고
    • Does Escherichia coli optimize the economics of the translation process?
    • Solomovici J, Lesnik T, Reiss C. 1997. Does Escherichia coli optimize the economics of the translation process? J Theor Biol 185:511-521.
    • (1997) J Theor Biol , vol.185 , pp. 511-521
    • Solomovici, J.1    Lesnik, T.2    Reiss, C.3
  • 18
    • 0031596205 scopus 로고    scopus 로고
    • Acylation of Escherichia coli hemolysin: A unique protein lipidation mechanism underlying toxin function
    • Stanley P, Koronakis V, Hughes C. 1998. Acylation of Escherichia coli hemolysin: A unique protein lipidation mechanism underlying toxin function. Microbiol Mol Biol Rev 62:309-333.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 309-333
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 19
    • 13544264496 scopus 로고    scopus 로고
    • Improved secretory production of recombinant proteins by random mutagenesis of hlyB, an alpha-hemolysin transporter from Escherichia coli
    • Sugamata Y, Shiba T. 2005. Improved secretory production of recombinant proteins by random mutagenesis of hlyB, an alpha-hemolysin transporter from Escherichia coli. Appl Environ Microbiol 71:656-662.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 656-662
    • Sugamata, Y.1    Shiba, T.2
  • 20
    • 0032538793 scopus 로고    scopus 로고
    • Substrate-induced assembly of a contiguous channel for protein export from E. coli: Reversible bridging of an inner-membrane translocase to an outer membrane exit pore
    • Thanabalu T, Koronakis E, Hughes C, Koronakis V. 1998. Substrate-induced assembly of a contiguous channel for protein export from E. coli: Reversible bridging of an inner-membrane translocase to an outer membrane exit pore. EMBO J 17:6487-6496.
    • (1998) EMBO J , vol.17 , pp. 6487-6496
    • Thanabalu, T.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 21
    • 0026761521 scopus 로고
    • A heterologous membrane protein domain fused to the C-terminal ATP-binding domain of HlyB can export Escherichia coli hemolysin
    • Thomas WD, Jr., Wagner SP, Welch RA. 1992. A heterologous membrane protein domain fused to the C-terminal ATP-binding domain of HlyB can export Escherichia coli hemolysin. J Bacteriol 174:6771-6779.
    • (1992) J Bacteriol , vol.174 , pp. 6771-6779
    • Thomas Jr., W.D.1    Wagner, S.P.2    Welch, R.A.3
  • 22
    • 0042193601 scopus 로고    scopus 로고
    • Protein aggregation in recombinant bacteria: Biological role of inclusion bodies
    • CarrioMM
    • Villaverde A, CarrioMM. 2003. Protein aggregation in recombinant bacteria: Biological role of inclusion bodies. Biotechnol Lett 25: 1385-1395.
    • (2003) Biotechnol Lett , vol.25 , pp. 1385-1395
    • Villaverde, A.1
  • 23
    • 33746163862 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks - 2006
    • Walsh G. 2006. Biopharmaceutical benchmarks - 2006. Nat Biotechnol 24:769-776.
    • (2006) Nat Biotechnol , vol.24 , pp. 769-776
    • Walsh, G.1
  • 24
    • 26644439939 scopus 로고    scopus 로고
    • jViz.Rna - A Java Tool for RNA Secondary Structure Visualization
    • Wiese KC, Glen E, Vasudevan A. 2005. jViz.Rna - A Java Tool for RNA Secondary Structure Visualization. IEEE Trans NanoBioscience 4:212-218.
    • (2005) IEEE Trans NanoBioscience , vol.4 , pp. 212-218
    • Wiese, K.C.1    Glen, E.2    Vasudevan, A.3
  • 25
    • 0023811932 scopus 로고
    • Design, synthesis and expression of a human interleukin-2 gene incorporating the codon usage bias found in highly expressed Escherichia coli genes
    • Williams DP, Regier D, Akiyoshi D, Genbauffe F, Murphy JR. 1988. Design, synthesis and expression of a human interleukin-2 gene incorporating the codon usage bias found in highly expressed Escherichia coli genes. Nucleic Acids Res 16:10453-10467.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10453-10467
    • Williams, D.P.1    Regier, D.2    Akiyoshi, D.3    Genbauffe, F.4    Murphy, J.R.5
  • 26
    • 30544435865 scopus 로고    scopus 로고
    • Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli
    • Zhang G, Brokx S, Weiner JH. 2006. Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli. Nat Biotechnol 24:100-104.
    • (2006) Nat Biotechnol , vol.24 , pp. 100-104
    • Zhang, G.1    Brokx, S.2    Weiner, J.H.3
  • 27
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M. 2003. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 31:3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.