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Volumn 417, Issue 2, 2009, Pages 477-483

A cysteine-rich metal-binding domain from rubella virus non-structural protein is essential for viral protease activity and virus replication

Author keywords

Conformational change; Fluorescence; Protease; Rubella virus (RUBV); Zinc binding protein

Indexed keywords

BINDING LIGANDS; BINDING MOTIF; CALCIUM IONS; CONFORMATIONAL CHANGE; DISSOCIATION CONSTANT; FLUORESCENCE METHOD; FLUORESCENCE QUENCHING; HYDROPHOBIC REGIONS; MATURE PROTEINS; METAL BINDING DOMAIN; MUTATIONAL ANALYSIS; OPTIMAL ACTIVITY; PROTEASE; PROTEOLYTIC ACTIVITIES; RUBELLA VIRUS (RUBV); SELF-CLEAVAGE; STRUCTURAL PROTEINS; SULFONIC ACID; VIRAL PROTEASE; VIRUS REPLICATION;

EID: 58249083483     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20081468     Document Type: Article
Times cited : (14)

References (34)
  • 1
    • 33747138073 scopus 로고    scopus 로고
    • The rubella virus nonstructural protease recognizes itself via an internal sequence present upstream of the cleavage site for trans-activity
    • Chen, H. H., Stark, C. J. and Atreya, C. D. (2006) The rubella virus nonstructural protease recognizes itself via an internal sequence present upstream of the cleavage site for trans-activity. Arch. Virol. 151, 1841-1851
    • (2006) Arch. Virol , vol.151 , pp. 1841-1851
    • Chen, H.H.1    Stark, C.J.2    Atreya, C.D.3
  • 2
    • 0029982325 scopus 로고    scopus 로고
    • Characterization of the rubella virus nonstructural protease domain and its cleavage site
    • Chen, J. P., Strauss, J. H., Strauss, E. G. and Frey, T. K. (1996) Characterization of the rubella virus nonstructural protease domain and its cleavage site. J. Virol. 70, 4707-4713
    • (1996) J. Virol , vol.70 , pp. 4707-4713
    • Chen, J.P.1    Strauss, J.H.2    Strauss, E.G.3    Frey, T.K.4
  • 4
    • 0031977295 scopus 로고    scopus 로고
    • The rubella virus nonstructural protease requires divalent cations for activity and functions in trans
    • Liu, X., Ropp, S. L., Jackson, R. J. and Frey, T. K. (1998) The rubella virus nonstructural protease requires divalent cations for activity and functions in trans. J. Virol. 72, 4463-4466
    • (1998) J. Virol , vol.72 , pp. 4463-4466
    • Liu, X.1    Ropp, S.L.2    Jackson, R.J.3    Frey, T.K.4
  • 5
    • 0034045399 scopus 로고    scopus 로고
    • Characterization of the zinc binding activity of the rubella virus nonstructural protease
    • Liu, X., Yang, J., Ghazi, A. M. and Frey, T. K. (2000) Characterization of the zinc binding activity of the rubella virus nonstructural protease. J. Virol. 74, 5949-5956
    • (2000) J. Virol , vol.74 , pp. 5949-5956
    • Liu, X.1    Yang, J.2    Ghazi, A.M.3    Frey, T.K.4
  • 6
    • 33645770271 scopus 로고    scopus 로고
    • Analysis of rubella virus capsid protein-mediated enhancement of replicon replication and mutant rescue
    • Tzeng, W. P., Matthews, J. D. and Frey, T. K. (2006) Analysis of rubella virus capsid protein-mediated enhancement of replicon replication and mutant rescue. J. Virol. 80, 3966-3974
    • (2006) J. Virol , vol.80 , pp. 3966-3974
    • Tzeng, W.P.1    Matthews, J.D.2    Frey, T.K.3
  • 7
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: Complexity in moderation
    • Mayer, B. J. (2001) SH3 domains: complexity in moderation. J. Cell Sci. 114, 1253-1263
    • (2001) J. Cell Sci , vol.114 , pp. 1253-1263
    • Mayer, B.J.1
  • 8
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C. and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326
    • (1989) Anal. Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 9
    • 0022051541 scopus 로고
    • The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase
    • Hunt, J. B., Neece, S. H. and Ginsburg, A. (1985) The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase. Anal. Biochem. 146, 150-157
    • (1985) Anal. Biochem , vol.146 , pp. 150-157
    • Hunt, J.B.1    Neece, S.H.2    Ginsburg, A.3
  • 10
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: Generation and refinement of homology-based protein structure models
    • Fiser, A. and Sali, A. (2003) Modeller: generation and refinement of homology-based protein structure models. Methods Enzymol. 374, 461-491
    • (2003) Methods Enzymol , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 11
    • 0026059140 scopus 로고
    • Structure of domain 1 of rat T lymphocyte CD2 antigen
    • Driscoll, P. C., Cyster, J. G., Campbell, I. D. and Williams, A. F. (1991) Structure of domain 1 of rat T lymphocyte CD2 antigen. Nature 353, 762-765
    • (1991) Nature , vol.353 , pp. 762-765
    • Driscoll, P.C.1    Cyster, J.G.2    Campbell, I.D.3    Williams, A.F.4
  • 12
    • 0034613018 scopus 로고    scopus 로고
    • Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes
    • Guarne, A., Hampoelz, B., Glaser, W., Carpena, X., Tormo, J., Fita, I. and Skern, T. (2000) Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes. J. Mol. Biol. 302, 1227-1240
    • (2000) J. Mol. Biol , vol.302 , pp. 1227-1240
    • Guarne, A.1    Hampoelz, B.2    Glaser, W.3    Carpena, X.4    Tormo, J.5    Fita, I.6    Skern, T.7
  • 14
    • 33847668459 scopus 로고    scopus 로고
    • Genomic analysis of diverse rubella virus genotypes
    • Zhou, Y., Ushijima, H. and Frey, T. K. (2007) Genomic analysis of diverse rubella virus genotypes. J. Gen. Virol. 88, 932-941
    • (2007) J. Gen. Virol , vol.88 , pp. 932-941
    • Zhou, Y.1    Ushijima, H.2    Frey, T.K.3
  • 15
    • 0034633293 scopus 로고    scopus 로고
    • Colorimetric and fluorimetric assays to quantitate micromolar concentrations of transition metals
    • McCall, K. A. and Fierke, C. A. (2000) Colorimetric and fluorimetric assays to quantitate micromolar concentrations of transition metals. Anal. Biochem. 284, 307-315
    • (2000) Anal. Biochem , vol.284 , pp. 307-315
    • McCall, K.A.1    Fierke, C.A.2
  • 16
    • 21644470326 scopus 로고    scopus 로고
    • Mutations in the putative zinc-binding motif of UL52 demonstrate a complex interdependence between the UL5 and UL52 subunits of the human herpes simplex virus type 1 helicase/primase complex
    • Chen, Y., Carrington-Lawrence, S. D., Bai, P. and Weller, S. K. (2005) Mutations in the putative zinc-binding motif of UL52 demonstrate a complex interdependence between the UL5 and UL52 subunits of the human herpes simplex virus type 1 helicase/primase complex. J. Virol. 79, 9088-9096
    • (2005) J. Virol , vol.79 , pp. 9088-9096
    • Chen, Y.1    Carrington-Lawrence, S.D.2    Bai, P.3    Weller, S.K.4
  • 17
    • 0029986494 scopus 로고    scopus 로고
    • Genetic analysis of the zinc finger in the Moloney murine leukemia virus nucleocapsid domain: Replacement of zinc-coordinating residues with other zinc-coordinating residues yields noninfectious particles containing genomic RNA
    • Gorelick, R. J., Chabot, D. J., Ott, D. E., Gagliardi, T. D., Rein, A., Henderson, L. E. and Arthur, L. O. (1996) Genetic analysis of the zinc finger in the Moloney murine leukemia virus nucleocapsid domain: replacement of zinc-coordinating residues with other zinc-coordinating residues yields noninfectious particles containing genomic RNA. J. Virol. 70, 2593-2597
    • (1996) J. Virol , vol.70 , pp. 2593-2597
    • Gorelick, R.J.1    Chabot, D.J.2    Ott, D.E.3    Gagliardi, T.D.4    Rein, A.5    Henderson, L.E.6    Arthur, L.O.7
  • 18
    • 19944384581 scopus 로고    scopus 로고
    • Single point mutations in the zinc finger motifs of the human immunodeficiency virus type 1 nucleocapsid alter RNA binding specificities of the gag protein and enhance packaging and infectivity
    • Mark-Danieli, M., Laham, N., Kenan-Eichler, M., Castiel, A., Melamed, D., Landau, M., Bouvier, N. M., Evans, M. J. and Bacharach, E. (2005) Single point mutations in the zinc finger motifs of the human immunodeficiency virus type 1 nucleocapsid alter RNA binding specificities of the gag protein and enhance packaging and infectivity. J. Virol. 79, 7756-7767
    • (2005) J. Virol , vol.79 , pp. 7756-7767
    • Mark-Danieli, M.1    Laham, N.2    Kenan-Eichler, M.3    Castiel, A.4    Melamed, D.5    Landau, M.6    Bouvier, N.M.7    Evans, M.J.8    Bacharach, E.9
  • 19
    • 0036432812 scopus 로고    scopus 로고
    • Mutational analysis of the Sendai virus V protein: Importance of the conserved residues for Zn binding, virus pathogenesis, and efficient RNA editing
    • Fukuhara, N., Huang, C., Kiyotani, K., Yoshida, T. and Sakaguchi, T. (2002) Mutational analysis of the Sendai virus V protein: importance of the conserved residues for Zn binding, virus pathogenesis, and efficient RNA editing. Virology 299, 172-181
    • (2002) Virology , vol.299 , pp. 172-181
    • Fukuhara, N.1    Huang, C.2    Kiyotani, K.3    Yoshida, T.4    Sakaguchi, T.5
  • 20
    • 33746846057 scopus 로고    scopus 로고
    • Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs
    • Joseph, J. S., Saikatendu, K. S., Subramanian, V., Neuman, B. W., Brooun, A., Griffith, M., Moy, K., Yadav, M. K., Velasquez, J., Buchmeier, M. J. et al. (2006) Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs. J. Virol. 80, 7894-7901
    • (2006) J. Virol , vol.80 , pp. 7894-7901
    • Joseph, J.S.1    Saikatendu, K.S.2    Subramanian, V.3    Neuman, B.W.4    Brooun, A.5    Griffith, M.6    Moy, K.7    Yadav, M.K.8    Velasquez, J.9    Buchmeier, M.J.10
  • 23
    • 19644393931 scopus 로고    scopus 로고
    • Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase
    • Tellinghuisen, T. L., Marcotrigiano, J. and Rice, C. M. (2005) Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase. Nature 435, 374-379
    • (2005) Nature , vol.435 , pp. 374-379
    • Tellinghuisen, T.L.1    Marcotrigiano, J.2    Rice, C.M.3
  • 24
    • 0037127306 scopus 로고    scopus 로고
    • Oligomeric interaction of hepatitis C virus NS5B is critical for catalytic activity of RNA-dependent RNA polymerase
    • Qin, W., Luo, H., Nomura, T., Hayashi, N., Yamashita, T. and Murakami, S. (2002) Oligomeric interaction of hepatitis C virus NS5B is critical for catalytic activity of RNA-dependent RNA polymerase. J. Biol. Chem. 277, 2132-2137
    • (2002) J. Biol. Chem , vol.277 , pp. 2132-2137
    • Qin, W.1    Luo, H.2    Nomura, T.3    Hayashi, N.4    Yamashita, T.5    Murakami, S.6
  • 25
    • 23044490251 scopus 로고    scopus 로고
    • Papain-like protease 2 (PLP2) from severe acute respiratory syndrome coronavirus (SARS-CoV): Expression, purification, characterization, and inhibition
    • Han, Y. S., Chang, G. G., Juo, C. G., Lee, H. J., Yeh, S. H., Hsu, J. T. and Chen, X. (2005) Papain-like protease 2 (PLP2) from severe acute respiratory syndrome coronavirus (SARS-CoV): expression, purification, characterization, and inhibition. Biochemistry 44, 10349-10359
    • (2005) Biochemistry , vol.44 , pp. 10349-10359
    • Han, Y.S.1    Chang, G.G.2    Juo, C.G.3    Lee, H.J.4    Yeh, S.H.5    Hsu, J.T.6    Chen, X.7
  • 26
    • 0035852649 scopus 로고    scopus 로고
    • A zinc finger-containing papain-like protease couples subgenomic mRNA synthesis to genome translation in a positive-stranded RNA virus
    • Tijms, M. A., van Dinten, L. C., Gorbalenya, A. E. and Snijder, E. J. (2001) A zinc finger-containing papain-like protease couples subgenomic mRNA synthesis to genome translation in a positive-stranded RNA virus. Proc. Natl. Acad. Sci. U.S.A. 98, 1889-1894
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 1889-1894
    • Tijms, M.A.1    van Dinten, L.C.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 27
    • 0035950926 scopus 로고    scopus 로고
    • Leader protein of encephalomyocarditis virus binds zinc, is phosphorylated during viral infection, and affects the efficiency of genome translation
    • Dvorak, C. M., Hall, D. J., Hill, M., Riddle, M., Pranter, A., Dillman, J., Deibel, M. and Palmenberg, A. C. (2001) Leader protein of encephalomyocarditis virus binds zinc, is phosphorylated during viral infection, and affects the efficiency of genome translation. Virology. 290, 261-271
    • (2001) Virology , vol.290 , pp. 261-271
    • Dvorak, C.M.1    Hall, D.J.2    Hill, M.3    Riddle, M.4    Pranter, A.5    Dillman, J.6    Deibel, M.7    Palmenberg, A.C.8
  • 28
    • 0033522886 scopus 로고    scopus 로고
    • The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism
    • Barbato, G., Cicero, D. O., Nardi, M. C., Steinkuhler, C., Cortese, R., De Francesco, R. and Bazzo, R. (1999) The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism. J. Mol. Biol. 289, 371-384
    • (1999) J. Mol. Biol , vol.289 , pp. 371-384
    • Barbato, G.1    Cicero, D.O.2    Nardi, M.C.3    Steinkuhler, C.4    Cortese, R.5    De Francesco, R.6    Bazzo, R.7
  • 30
    • 0017278562 scopus 로고
    • Role of calcium ions in the thermostability of thermolysin and Bacillus subtilis var. amylosacchariticus neutral protease
    • Tajima, M., Urabe, I., Yutani, K. and Okada, H. (1976) Role of calcium ions in the thermostability of thermolysin and Bacillus subtilis var. amylosacchariticus neutral protease. Eur. J. Biochem. 64, 243-247
    • (1976) Eur. J. Biochem , vol.64 , pp. 243-247
    • Tajima, M.1    Urabe, I.2    Yutani, K.3    Okada, H.4
  • 31
    • 0031766374 scopus 로고    scopus 로고
    • The hepatitis C virus NS3 proteinase: Structure and function of a zinc-containing serine proteinase
    • De Francesco, R., Pessi, A. and Steinkuhler, C. (1998) The hepatitis C virus NS3 proteinase: structure and function of a zinc-containing serine proteinase. Antivir. Ther. 3, 99-109
    • (1998) Antivir. Ther , vol.3 , pp. 99-109
    • De Francesco, R.1    Pessi, A.2    Steinkuhler, C.3
  • 32
    • 33846809096 scopus 로고    scopus 로고
    • Characterisation of the role of zinc in the hepatitis C virus NS2/3 auto-cleavage and NS3 protease activities
    • Tedbury, P. R. and Harris, M. (2007) Characterisation of the role of zinc in the hepatitis C virus NS2/3 auto-cleavage and NS3 protease activities. J. Mol. Biol. 366, 1652-1660
    • (2007) J. Mol. Biol , vol.366 , pp. 1652-1660
    • Tedbury, P.R.1    Harris, M.2
  • 33
    • 29744455503 scopus 로고    scopus 로고
    • The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity
    • Barretto, N., Jukneliene, D., Ratia, K., Chen, Z., Mesecar, A. D. and Baker, S. C. (2005) The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity. J. Virol. 79, 15189-15198
    • (2005) J. Virol , vol.79 , pp. 15189-15198
    • Barretto, N.1    Jukneliene, D.2    Ratia, K.3    Chen, Z.4    Mesecar, A.D.5    Baker, S.C.6


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