메뉴 건너뛰기




Volumn 365, Issue 1, 2007, Pages 79-91

Significance of the C-terminal amino acid residue in mengovirus RNA-dependent RNA polymerase

Author keywords

Cardioviruses; Mengovirus; Mutations; RNA dependent RNA polymerase; Structure modeling

Indexed keywords

ALANINE; AMINO ACID; ARGININE; HISTONE; ISOLEUCINE; LEUCINE; PHENYLALANINE; RNA POLYMERASE; SERINE; TRYPTOPHAN; TYROSINE; VALINE; VIRUS RNA;

EID: 34250160913     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2007.02.038     Document Type: Article
Times cited : (10)

References (44)
  • 2
    • 33750568984 scopus 로고    scopus 로고
    • Site-directed mutagenesis and 3D structure modeling reveal the functional role of C-terminalTrp460 of mengoviral RNA-dependent RNA polymerase
    • Alexeevski A.V., Dmitrieva T.M., Shatskaya G.S., Markouchevitch D., and Tolskaya E.A. Site-directed mutagenesis and 3D structure modeling reveal the functional role of C-terminalTrp460 of mengoviral RNA-dependent RNA polymerase. Biofizika 48 Suppl. 1 (2003) S167-S178
    • (2003) Biofizika , vol.48 , Issue.SUPPL. 1
    • Alexeevski, A.V.1    Dmitrieva, T.M.2    Shatskaya, G.S.3    Markouchevitch, D.4    Tolskaya, E.A.5
  • 4
    • 0023756753 scopus 로고
    • A sequence motif in many polymerases
    • Argos P. A sequence motif in many polymerases. Nucleic Acid Res. 16 (1988) 9909-9916
    • (1988) Nucleic Acid Res. , vol.16 , pp. 9909-9916
    • Argos, P.1
  • 5
    • 23744436747 scopus 로고    scopus 로고
    • Crystal structures of the RNA-dependent RNA polymerase genotype 2a of hepatitis C virus reveal two conformations and suggest mechanisms of inhibition by non-nucleoside inhibitors
    • Biswal B.K., Cherney M.M., Wang M., Chan L., Yannopoulos C.G., Bilimoria D., Nicolas O., Bedard J., and James M.N. Crystal structures of the RNA-dependent RNA polymerase genotype 2a of hepatitis C virus reveal two conformations and suggest mechanisms of inhibition by non-nucleoside inhibitors. J. Biol. Chem. 280 (2005) 18202-18210
    • (2005) J. Biol. Chem. , vol.280 , pp. 18202-18210
    • Biswal, B.K.1    Cherney, M.M.2    Wang, M.3    Chan, L.4    Yannopoulos, C.G.5    Bilimoria, D.6    Nicolas, O.7    Bedard, J.8    James, M.N.9
  • 7
    • 0037386414 scopus 로고    scopus 로고
    • A structural and primary sequence comparison of the viral RNA-dependent RNA polymerases
    • Bruenn J.A. A structural and primary sequence comparison of the viral RNA-dependent RNA polymerases. Nucleic Acids Res. 31 (2003) 1821-1829
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1821-1829
    • Bruenn, J.A.1
  • 8
    • 0033732321 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray chrystallographic studies on the bacteriophage φ{symbol}6 RNA-dependent RNA polymerase
    • Butcher S.J., Makeyev E.V., Grimes J.M., Stuart D.I., and Bamford D.H. Crystallization and preliminary X-ray chrystallographic studies on the bacteriophage φ{symbol}6 RNA-dependent RNA polymerase. Acta Crystallogr., D. 56 (2000) 1473-1475
    • (2000) Acta Crystallogr., D. , vol.56 , pp. 1473-1475
    • Butcher, S.J.1    Makeyev, E.V.2    Grimes, J.M.3    Stuart, D.I.4    Bamford, D.H.5
  • 10
    • 0141847908 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3D-pol): structure, function, and mechanism
    • Semler B.L., and Wimmer E. (Eds), ASM Press, Washington, DC
    • Cameron C.E., Gohara D.W., and Arnold J.J. Poliovirus RNA-dependent RNA polymerase (3D-pol): structure, function, and mechanism. In: Semler B.L., and Wimmer E. (Eds). Molecular Biology of Picornaviruses (2002), ASM Press, Washington, DC 255-267
    • (2002) Molecular Biology of Picornaviruses , pp. 255-267
    • Cameron, C.E.1    Gohara, D.W.2    Arnold, J.J.3
  • 11
    • 1842481188 scopus 로고    scopus 로고
    • The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation
    • Choi K.H., Groarke J.M., Young D.C., Kuhn R.J., Smith J.L., Pevear D.C., and Rossmann M.G. The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 4425-4430
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 4425-4430
    • Choi, K.H.1    Groarke, J.M.2    Young, D.C.3    Kuhn, R.J.4    Smith, J.L.5    Pevear, D.C.6    Rossmann, M.G.7
  • 12
    • 0024507859 scopus 로고
    • Cloning and synthesis of infectious cardiovirus RNAs containing short, discrete poly(C) tracts
    • Duke G.M., and Palmenberg A.C. Cloning and synthesis of infectious cardiovirus RNAs containing short, discrete poly(C) tracts. J. Virol. 63 (1989) 1822-1826
    • (1989) J. Virol. , vol.63 , pp. 1822-1826
    • Duke, G.M.1    Palmenberg, A.C.2
  • 13
    • 8744222695 scopus 로고    scopus 로고
    • Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA
    • Ferrer-Orta C., Arias A., Perez-Luque R., Escarmis C., Domingo E., and Verdaguer N. Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA. J. Biol. Chem. 279 (2004) 47212-47221
    • (2004) J. Biol. Chem. , vol.279 , pp. 47212-47221
    • Ferrer-Orta, C.1    Arias, A.2    Perez-Luque, R.3    Escarmis, C.4    Domingo, E.5    Verdaguer, N.6
  • 17
    • 0031792943 scopus 로고    scopus 로고
    • Geometric invariant core for the V(L) and V(H) domains of immunoglobulin molecules
    • Gelfand I., Kister A., Kulikowski C., and Stoyanov O. Geometric invariant core for the V(L) and V(H) domains of immunoglobulin molecules. Protein Eng. 11 (1998) 1015-1125
    • (1998) Protein Eng. , vol.11 , pp. 1015-1125
    • Gelfand, I.1    Kister, A.2    Kulikowski, C.3    Stoyanov, O.4
  • 18
    • 34250164754 scopus 로고    scopus 로고
    • Life Core, the program for classification of macromolecular complexes
    • Gribkov M., Alexeevski A., Ivanova D., Karyagina A., and Spirin S. Life Core, the program for classification of macromolecular complexes. Biofizika (Moscow) 48 Suppl. 1 (2004) 157-166
    • (2004) Biofizika (Moscow) , vol.48 , Issue.SUPPL. 1 , pp. 157-166
    • Gribkov, M.1    Alexeevski, A.2    Ivanova, D.3    Karyagina, A.4    Spirin, S.5
  • 19
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 20
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen J.L., Long A.M., and Schultz S.C. Structure of the RNA-dependent RNA polymerase of poliovirus. Structure 5 (1997) 1109-1122
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 22
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance
    • Huang H., Chopra R., Verdine G.L., and Harrison S.C. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science 282 (1998) 1669-1675
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 24
    • 0025743809 scopus 로고
    • The phylogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses
    • Koonin E.V. The phylogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses. J. Gen. Virol. 72 (1991) 2197-2206
    • (1991) J. Gen. Virol. , vol.72 , pp. 2197-2206
    • Koonin, E.V.1
  • 25
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T.A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. U.S.A. 82 (1985) 488-492
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 26
    • 0032876683 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus. reveals a fully encircled active site
    • Lesburg C.A., Cable M.B., Ferrari E., Hong Z., Mannarino A.F., and Weber P.C. Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus. reveals a fully encircled active site. Nat. Struct. Biol. 6 (1999) 937-943
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 937-943
    • Lesburg, C.A.1    Cable, M.B.2    Ferrari, E.3    Hong, Z.4    Mannarino, A.F.5    Weber, P.C.6
  • 27
    • 0041707714 scopus 로고    scopus 로고
    • Identification of a C-Terminal regulatory motif in hepatitis C virus RNA-dependent RNA polymerase: structural and biochemical analysis
    • Lévêque V.J.-P., Johnson R.B., Parsons S., Ren J., Xie C., Zhang F., and Wang Q.M. Identification of a C-Terminal regulatory motif in hepatitis C virus RNA-dependent RNA polymerase: structural and biochemical analysis. J. Virol. 77 (2003) 9020-9028
    • (2003) J. Virol. , vol.77 , pp. 9020-9028
    • Lévêque, V.J.-P.1    Johnson, R.B.2    Parsons, S.3    Ren, J.4    Xie, C.5    Zhang, F.6    Wang, Q.M.7
  • 28
    • 4143147318 scopus 로고    scopus 로고
    • The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: a dual function target for common cold antiviral therapy
    • Love R.A., Maegley K.A., Yu X., Ferre R.A., Lingardo L.K., Diehl W., Parge H.E., Dragovich P.S., and Fuhrman S.A. The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: a dual function target for common cold antiviral therapy. Structure 12 (2004) 1533-1544
    • (2004) Structure , vol.12 , pp. 1533-1544
    • Love, R.A.1    Maegley, K.A.2    Yu, X.3    Ferre, R.A.4    Lingardo, L.K.5    Diehl, W.6    Parge, H.E.7    Dragovich, P.S.8    Fuhrman, S.A.9
  • 29
    • 0037059758 scopus 로고    scopus 로고
    • Crystal structures of active and inactive conformations of a caliciviral RNA-dependent RNA polymerase
    • Ng K.K., Cherney M.M., Vazquez A.L., Machin A., Alonso J.M.M., Parra F., and James M.N.G. Crystal structures of active and inactive conformations of a caliciviral RNA-dependent RNA polymerase. J. Biol. Chem. 277 (2002) 1381-1387
    • (2002) J. Biol. Chem. , vol.277 , pp. 1381-1387
    • Ng, K.K.1    Cherney, M.M.2    Vazquez, A.L.3    Machin, A.4    Alonso, J.M.M.5    Parra, F.6    James, M.N.G.7
  • 30
    • 1942501581 scopus 로고    scopus 로고
    • Crystal structure of Norwalk virus polymerase reveals the carboxyl terminus in the active site cleft
    • Ng K.K., Pendas-Franco N., Rojo J., Boga J.A., Machin A., Alonso J.M., and Parra F. Crystal structure of Norwalk virus polymerase reveals the carboxyl terminus in the active site cleft. J. Biol. Chem. 279 (2004) 16638-16645
    • (2004) J. Biol. Chem. , vol.279 , pp. 16638-16645
    • Ng, K.K.1    Pendas-Franco, N.2    Rojo, J.3    Boga, J.A.4    Machin, A.5    Alonso, J.M.6    Parra, F.7
  • 32
    • 0037470586 scopus 로고    scopus 로고
    • Substrate complexes of hepatitis C virus RNA polymerase (HC-J4): structural evidence for nucleotide import and de-novo initiation
    • O'Farrell D., Trowbridge R., Rowlands D., and Jager J. Substrate complexes of hepatitis C virus RNA polymerase (HC-J4): structural evidence for nucleotide import and de-novo initiation. J. Mol. Biol. 326 (2003) 1025-1035
    • (2003) J. Mol. Biol. , vol.326 , pp. 1025-1035
    • O'Farrell, D.1    Trowbridge, R.2    Rowlands, D.3    Jager, J.4
  • 33
    • 0032567393 scopus 로고    scopus 로고
    • Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions
    • O'Reilly E.K., and Kao C.C. Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions. Virology 252 (1998) 287-303
    • (1998) Virology , vol.252 , pp. 287-303
    • O'Reilly, E.K.1    Kao, C.C.2
  • 34
    • 0029330222 scopus 로고
    • Functional oligomerization of poliovirus RNA-dependent RNA polymerase
    • Pata J.D., Schultz S.C., and Kirkegaard K. Functional oligomerization of poliovirus RNA-dependent RNA polymerase. RNA 1 (1995) 466-477
    • (1995) RNA , vol.1 , pp. 466-477
    • Pata, J.D.1    Schultz, S.C.2    Kirkegaard, K.3
  • 35
    • 0024784519 scopus 로고
    • Identification of four conserved motifs among the RNA-dependent polymerase encoding elements
    • Poch O., Sauvaget I., Delarue M., and Tordo N. Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. EMBO J. 8 (1989) 3867-3874
    • (1989) EMBO J. , vol.8 , pp. 3867-3874
    • Poch, O.1    Sauvaget, I.2    Delarue, M.3    Tordo, N.4
  • 38
    • 0026783262 scopus 로고
    • Point mutations which drastically affect the polymerisation activity of encephalomyocarditis virus RNA-dependent RNA polymerase correspond to the active site of Escherichia coli DNA polymerase I
    • Sankar S., and Porter A.G. Point mutations which drastically affect the polymerisation activity of encephalomyocarditis virus RNA-dependent RNA polymerase correspond to the active site of Escherichia coli DNA polymerase I. J. Biol. Chem. 268 (1992) 10168-10176
    • (1992) J. Biol. Chem. , vol.268 , pp. 10168-10176
    • Sankar, S.1    Porter, A.G.2
  • 40
    • 0038754497 scopus 로고    scopus 로고
    • Semler B.L., and Wimmer E. (Eds), ASM Press, Washington, DC
    • In: Semler B.L., and Wimmer E. (Eds). Molecular Biology of Picornaviruses (2002), ASM Press, Washington, DC
    • (2002) Molecular Biology of Picornaviruses
  • 41
    • 0003408570 scopus 로고
    • IRL Press, Oxford http://www.biochem.ucl.ac.uk/bsm/sidechains/Trp/Thr/sindex.html
    • Singh J., and Thornton J.M. Atlas of Protein Side-Chain Interactions vols. I & II (1992), IRL Press, Oxford. http://www.biochem.ucl.ac.uk/bsm/sidechains/Trp/Thr/sindex.html http://www.biochem.ucl.ac.uk/bsm/sidechains/Trp/Thr/sindex.html
    • (1992) Atlas of Protein Side-Chain Interactions , vol.I - II
    • Singh, J.1    Thornton, J.M.2
  • 42
    • 18744392514 scopus 로고    scopus 로고
    • RNA synthesis in a cage-structural studies of reovirus polymerase lambda3
    • Tao Y., Farsetta D.L., Nibert M.L., and Harrison S.C. RNA synthesis in a cage-structural studies of reovirus polymerase lambda3. Cell 111 (2002) 733-745
    • (2002) Cell , vol.111 , pp. 733-745
    • Tao, Y.1    Farsetta, D.L.2    Nibert, M.L.3    Harrison, S.C.4
  • 43
    • 4644238112 scopus 로고    scopus 로고
    • Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase
    • Thompson A.A., and Peersen O.B. Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase. EMBO J. 23 (2004) 3462-3471
    • (2004) EMBO J. , vol.23 , pp. 3462-3471
    • Thompson, A.A.1    Peersen, O.B.2
  • 44
    • 2442677715 scopus 로고    scopus 로고
    • Initiation of viral RNA-dependent RNA polymerization
    • van Dijk A.A., Makeyev E.V., and Bamford D.H. Initiation of viral RNA-dependent RNA polymerization. J. Gen. Virol. 85 (2004) 1077-1093
    • (2004) J. Gen. Virol. , vol.85 , pp. 1077-1093
    • van Dijk, A.A.1    Makeyev, E.V.2    Bamford, D.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.