메뉴 건너뛰기




Volumn 53, Issue 1, 2007, Pages 132-137

Identification and characterization of a +1 frameshift observed during the expression of Epstein-Barr virus IL-10 in Escherichia coli

Author keywords

Epstein Barr virus; Escherichia coli; Frameshift; IL 10

Indexed keywords

ARGININE TRANSFER RNA; COMPLEMENTARY DNA; INTERLEUKIN 10; PEPTIDE FRAGMENT; TRYPSIN;

EID: 33847101310     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.12.001     Document Type: Article
Times cited : (6)

References (26)
  • 2
    • 0026000892 scopus 로고
    • Interleukin 10 (IL-10) and viral IL-10 strongly reduce antigen-specific human T cell proliferation by diminishing the antigen-presenting capacity of monocytes via downregulation of class II major histocompatibility complex expression
    • de Waal Malefyt R., Haanen J., Spits H., Roncarolo M.G., te Velde A., Figdor C., Johnson K., Kastelein R., Yssel H., and de Vries J.E. Interleukin 10 (IL-10) and viral IL-10 strongly reduce antigen-specific human T cell proliferation by diminishing the antigen-presenting capacity of monocytes via downregulation of class II major histocompatibility complex expression. J. Exp. Med. 174 (1991) 915-924
    • (1991) J. Exp. Med. , vol.174 , pp. 915-924
    • de Waal Malefyt, R.1    Haanen, J.2    Spits, H.3    Roncarolo, M.G.4    te Velde, A.5    Figdor, C.6    Johnson, K.7    Kastelein, R.8    Yssel, H.9    de Vries, J.E.10
  • 3
    • 0026094306 scopus 로고
    • Interleukin 10 (IL-10) inhibits cytokine synthesis by human monocytes: an autoregulatory role of IL-10 produced by monocytes
    • de Waal Malefyt R., Abrams J., Bennett B., Figdor C.G., and de Vries J.E. Interleukin 10 (IL-10) inhibits cytokine synthesis by human monocytes: an autoregulatory role of IL-10 produced by monocytes. J. Exp. Med. 174 (1991) 1209-1220
    • (1991) J. Exp. Med. , vol.174 , pp. 1209-1220
    • de Waal Malefyt, R.1    Abrams, J.2    Bennett, B.3    Figdor, C.G.4    de Vries, J.E.5
  • 4
    • 0025610845 scopus 로고
    • IL-10, a novel growth cofactor for mature and immature T cells
    • MacNeil I.A., Suda T., Moore K.W., Mosmann T.R., and Zlotnik A. IL-10, a novel growth cofactor for mature and immature T cells. J. Immunol. 145 (1990) 4167-4173
    • (1990) J. Immunol. , vol.145 , pp. 4167-4173
    • MacNeil, I.A.1    Suda, T.2    Moore, K.W.3    Mosmann, T.R.4    Zlotnik, A.5
  • 6
    • 0034677006 scopus 로고    scopus 로고
    • A single amino acid determines the immunostimulatory activity of interleukin 10
    • Ding Y., Qin L., Kotenko S.V., Pestka S., and Bromberg J.S. A single amino acid determines the immunostimulatory activity of interleukin 10. J. Exp. Med. 191 (2000) 213-224
    • (2000) J. Exp. Med. , vol.191 , pp. 213-224
    • Ding, Y.1    Qin, L.2    Kotenko, S.V.3    Pestka, S.4    Bromberg, J.S.5
  • 7
    • 0035892751 scopus 로고    scopus 로고
    • Differential IL-10R1 expression plays a critical role in IL-10-mediated immune regulation
    • Ding Y., Qin L., Zamarin D., Kotenko S.V., Pestka S., Moore K.W., and Bromberg J.S. Differential IL-10R1 expression plays a critical role in IL-10-mediated immune regulation. J. Immunol. 167 (2001) 6884-6892
    • (2001) J. Immunol. , vol.167 , pp. 6884-6892
    • Ding, Y.1    Qin, L.2    Zamarin, D.3    Kotenko, S.V.4    Pestka, S.5    Moore, K.W.6    Bromberg, J.S.7
  • 8
    • 0031547973 scopus 로고    scopus 로고
    • Crystal structure of Epstein-Barr virus protein BCRF1, a homolog of cellular interleukin-10
    • Zdanov A., Schalk-Hihi C., Menon S., Moore K.W., and Wlodawer A. Crystal structure of Epstein-Barr virus protein BCRF1, a homolog of cellular interleukin-10. J. Mol. Biol. 268 (1997) 460-467
    • (1997) J. Mol. Biol. , vol.268 , pp. 460-467
    • Zdanov, A.1    Schalk-Hihi, C.2    Menon, S.3    Moore, K.W.4    Wlodawer, A.5
  • 9
    • 0029644946 scopus 로고
    • Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma
    • Zdanov A., Schalk-Hihi C., Gustchina A., Tsang M., Weatherbee J., and Wlodawer A. Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma. Structure 3 (1995) 591-601
    • (1995) Structure , vol.3 , pp. 591-601
    • Zdanov, A.1    Schalk-Hihi, C.2    Gustchina, A.3    Tsang, M.4    Weatherbee, J.5    Wlodawer, A.6
  • 10
    • 0029148581 scopus 로고
    • Crystal structure of interleukin 10 reveals an interferon gamma-like fold
    • Walter M.R., and Nagabhushan T.L. Crystal structure of interleukin 10 reveals an interferon gamma-like fold. Biochemistry 34 (1995) 12118-12125
    • (1995) Biochemistry , vol.34 , pp. 12118-12125
    • Walter, M.R.1    Nagabhushan, T.L.2
  • 13
    • 17044411254 scopus 로고    scopus 로고
    • Same structure, different function: Crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain
    • Yoon S.I., Jones B.C., Logsdon N.J., and Walter M.R. Same structure, different function: Crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain. Structure 13 (2005) 551-564
    • (2005) Structure , vol.13 , pp. 551-564
    • Yoon, S.I.1    Jones, B.C.2    Logsdon, N.J.3    Walter, M.R.4
  • 14
    • 33845948477 scopus 로고    scopus 로고
    • Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex
    • Yoon S.I., Logsdon N.J., Sheikh F., Donnelly R.P., and Walter M.R. Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex. J. Biol. Chem. 281 (2006) 35088-35096
    • (2006) J. Biol. Chem. , vol.281 , pp. 35088-35096
    • Yoon, S.I.1    Logsdon, N.J.2    Sheikh, F.3    Donnelly, R.P.4    Walter, M.R.5
  • 15
    • 0036065431 scopus 로고    scopus 로고
    • Noncompetitive antibody neutralization of IL-10 revealed by protein engineering and x-ray crystallography
    • Josephson K., Jones B.C., Walter L.J., DiGiacomo R., Indelicato S.R., and Walter M.R. Noncompetitive antibody neutralization of IL-10 revealed by protein engineering and x-ray crystallography. Structure 10 (2002) 981-987
    • (2002) Structure , vol.10 , pp. 981-987
    • Josephson, K.1    Jones, B.C.2    Walter, L.J.3    DiGiacomo, R.4    Indelicato, S.R.5    Walter, M.R.6
  • 17
    • 0029896020 scopus 로고    scopus 로고
    • Recoding: dynamic reprogramming of translation
    • Gesteland R.F., and Atkins J.F. Recoding: dynamic reprogramming of translation. Annu. Rev. Biochem. 65 (1996) 741-768
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 741-768
    • Gesteland, R.F.1    Atkins, J.F.2
  • 18
    • 0030271498 scopus 로고    scopus 로고
    • Errors of heterologous protein expression
    • Kurland C., and Gallant J. Errors of heterologous protein expression. Curr. Opin. Biotechnol. 7 (1996) 489-493
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 489-493
    • Kurland, C.1    Gallant, J.2
  • 20
    • 0027078856 scopus 로고
    • Novel in-frame two codon translational hop during synthesis of bovine placental lactogen in a recombinant strain of Escherichia coli
    • Kane J.F., Violand B.N., Curran D.F., Staten N.R., Duffin K.L., and Bogosian G. Novel in-frame two codon translational hop during synthesis of bovine placental lactogen in a recombinant strain of Escherichia coli. Nucleic Acids Res. 20 (1992) 6707-6712
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6707-6712
    • Kane, J.F.1    Violand, B.N.2    Curran, D.F.3    Staten, N.R.4    Duffin, K.L.5    Bogosian, G.6
  • 21
    • 0027513392 scopus 로고
    • Effects of consecutive AGG codons on translation in Escherichia coli, demonstrated with a versatile codon test system
    • Rosenberg A.H., Goldman E., Dunn J.J., Studier F.W., and Zubay G. Effects of consecutive AGG codons on translation in Escherichia coli, demonstrated with a versatile codon test system. J. Bacteriol. 175 (1993) 716-722
    • (1993) J. Bacteriol. , vol.175 , pp. 716-722
    • Rosenberg, A.H.1    Goldman, E.2    Dunn, J.J.3    Studier, F.W.4    Zubay, G.5
  • 22
    • 0030564828 scopus 로고    scopus 로고
    • Co-variation of tRNA abundance and codon usage in Escherichia coli at different growth rates
    • Dong H., Nilsson L., and Kurland C.G. Co-variation of tRNA abundance and codon usage in Escherichia coli at different growth rates. J. Mol. Biol. 260 (1996) 649-663
    • (1996) J. Mol. Biol. , vol.260 , pp. 649-663
    • Dong, H.1    Nilsson, L.2    Kurland, C.G.3
  • 23
    • 0141442962 scopus 로고    scopus 로고
    • Overcoming the codon bias of E. coli for enhanced protein expression
    • Novy R., Drott D., Yaeger K., and Mierendorf R. Overcoming the codon bias of E. coli for enhanced protein expression. InNovations 12 (2001) 1-3
    • (2001) InNovations , vol.12 , pp. 1-3
    • Novy, R.1    Drott, D.2    Yaeger, K.3    Mierendorf, R.4
  • 24
    • 33748316617 scopus 로고    scopus 로고
    • mRNA secondary structure at start AUG codon is a key limiting factor for human protein expression in Escherichia coli
    • Zhang W., Xiao W., Wei H., Zhang J., and Tian Z. mRNA secondary structure at start AUG codon is a key limiting factor for human protein expression in Escherichia coli. Biochem. Biophys. Res. Commun. 349 (2006) 69-78
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 69-78
    • Zhang, W.1    Xiao, W.2    Wei, H.3    Zhang, J.4    Tian, Z.5
  • 25
    • 0000516715 scopus 로고
    • Translation of the sequence AGG-AGG yields 50% ribosomal frameshift
    • Spanjaard R.A., and van Duin J. Translation of the sequence AGG-AGG yields 50% ribosomal frameshift. Proc. Natl. Acad. Sci. USA 85 (1988) 7967-7971
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7967-7971
    • Spanjaard, R.A.1    van Duin, J.2
  • 26
    • 0029773416 scopus 로고    scopus 로고
    • Three, four or more: the translational stop signal at length
    • Tate W.P., and Mannering S.A. Three, four or more: the translational stop signal at length. Mol. Microbiol. 21 (1996) 213-219
    • (1996) Mol. Microbiol. , vol.21 , pp. 213-219
    • Tate, W.P.1    Mannering, S.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.