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Volumn 86, Issue 14, 2012, Pages 7565-7576

Crystal structure of the superfamily 1 helicase from Tomato mosaic virus

Author keywords

[No Author keywords available]

Indexed keywords

HELICASE; PROTEIN ARL8; PROTEIN TOM1; RECA PROTEIN; UNCLASSIFIED DRUG; VIRUS ENZYME; VIRUS PROTEIN; VIRUS RNA;

EID: 84863760243     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00118-12     Document Type: Article
Times cited : (48)

References (53)
  • 1
    • 77952974276 scopus 로고    scopus 로고
    • Helicases: an overview
    • Abdelhaleem M. 2010. Helicases: an overview. Methods Mol. Biol. 587: 1-12.
    • (2010) Methods Mol. Biol. , vol.587 , pp. 1-12
    • Abdelhaleem, M.1
  • 2
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement
    • Adams PD, Pannu NS, Read RJ, Brunger AT. 1997. Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement. Proc. Natl. Acad. Sci. U. S. A. 94:5018 -5023.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5018-5023
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brunger, A.T.4
  • 5
    • 33846186825 scopus 로고    scopus 로고
    • Structural and functional insights into the human Upf1 helicase core
    • Cheng Z, Muhlrad D, Lim MK, Parker R, Song H. 2007. Structural and functional insights into the human Upf1 helicase core. EMBO J. 26:253- 264.
    • (2007) EMBO J , vol.26 , pp. 253-264
    • Cheng, Z.1    Muhlrad, D.2    Lim, M.K.3    Parker, R.4    Song, H.5
  • 6
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole C, Barber JD, Barton GJ. 2008. The Jpred 3 secondary structure prediction server. Nucleic Acids Res. 36:W197-W201.
    • (2008) Nucleic Acids Res , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 8
    • 0002648903 scopus 로고    scopus 로고
    • The helicase domain of the TMV replicase proteins induces the N-mediated defence response in tobacco
    • Erickson FL, et al. 1999. The helicase domain of the TMV replicase proteins induces the N-mediated defence response in tobacco. Plant J. 18:67-75.
    • (1999) Plant J , vol.18 , pp. 67-75
    • Erickson, F.L.1
  • 10
    • 0000751742 scopus 로고
    • Nucleotide sequence of tobacco mosaic virus RNA
    • Goelet P, et al. 1982. Nucleotide sequence of tobacco mosaic virus RNA. Proc. Natl. Acad. Sci. U. S. A. 79:5818 -5822.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 5818-5822
    • Goelet, P.1
  • 11
    • 0027182114 scopus 로고
    • Helicases: amino acid sequence comparisons and structure-function relationships
    • Gorbalenya AE, Koonin EV. 1993. Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 3:419-429.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 12
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
    • Gorbalenya AE, Koonin EV, Donchenko AP, Blinov VM. 1989. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 17:4713- 4730.
    • (1989) Nucleic Acids Res , vol.17 , pp. 4713-4730
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 13
    • 0035836370 scopus 로고    scopus 로고
    • Identification and functional analysis of an interaction between domains of the 126/183-kDa replicase-associated proteins of tobacco mosaic virus
    • Goregaoker SP, Lewandowski DJ, Culver JN. 2001. Identification and functional analysis of an interaction between domains of the 126/183-kDa replicase-associated proteins of tobacco mosaic virus. Virology 282:320- 328.
    • (2001) Virology , vol.282 , pp. 320-328
    • Goregaoker, S.P.1    Lewandowski, D.J.2    Culver, J.N.3
  • 14
    • 13844254123 scopus 로고    scopus 로고
    • Binding and unwinding: SF3 viral helicases
    • Hickman AB, Dyda F. 2005. Binding and unwinding: SF3 viral helicases. Curr. Opin. Struct. Biol. 15:77- 85.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 77-85
    • Hickman, A.B.1    Dyda, F.2
  • 15
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenstrom P. 2010. Dali server: conservation mapping in 3D. Nucleic Acids Res. 38:W545-W549.
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 17
    • 78149335264 scopus 로고    scopus 로고
    • Interactions between tobamovirus replication proteins and cellular factors: their impacts on virus multiplication
    • Ishibashi K, Nishikiori M, Ishikawa M. 2010. Interactions between tobamovirus replication proteins and cellular factors: their impacts on virus multiplication. Mol. Plant Microbe Interact. 23:1413-1419.
    • (2010) Mol. Plant Microbe Interact. , vol.23 , pp. 1413-1419
    • Ishibashi, K.1    Nishikiori, M.2    Ishikawa, M.3
  • 18
    • 0026002497 scopus 로고
    • Isolation of mutants of Arabidopsis thaliana in which accumulation of tobacco mosaic virus coat protein is reduced to low levels
    • Ishikawa M, Obata F, Kumagai T, Ohno T. 1991. Isolation of mutants of Arabidopsis thaliana in which accumulation of tobacco mosaic virus coat protein is reduced to low levels. Mol. Gen. Genet. 230:33-38.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 33-38
    • Ishikawa, M.1    Obata, F.2    Kumagai, T.3    Ohno, T.4
  • 19
    • 78650854687 scopus 로고    scopus 로고
    • RNA helicases at work: binding and rearranging
    • Jankowsky E. 2011. RNA helicases at work: binding and rearranging. Trends Biochem. Sci. 36:19 -29.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 19-29
    • Jankowsky, E.1
  • 20
    • 0030897821 scopus 로고    scopus 로고
    • Virus-encoded RNA helicases
    • Kadare G, Haenni AL. 1997. Virus-encoded RNA helicases. J. Virol. 71:2583-2590.
    • (1997) J. Virol. , vol.71 , pp. 2583-2590
    • Kadare, G.1    Haenni, A.L.2
  • 21
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding
    • Kim JL, et al. 1998. Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure 6:89 -100.
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1
  • 22
    • 16044364658 scopus 로고    scopus 로고
    • Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide
    • Kim JL, et al. 1996. Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide. Cell 87:343- 355.
    • (1996) Cell , vol.87 , pp. 343-355
    • Kim, J.L.1
  • 23
    • 51649095289 scopus 로고    scopus 로고
    • RNA interference screen for human genes associated with West Nile virus infection
    • Krishnan MN, et al. 2008. RNA interference screen for human genes associated with West Nile virus infection. Nature 455:242-245.
    • (2008) Nature , vol.455 , pp. 242-245
    • Krishnan, M.N.1
  • 24
    • 0141789662 scopus 로고    scopus 로고
    • Tomato mosaic virus replication protein suppresses virus-targeted posttranscriptional gene silencing
    • Kubota K, Tsuda S, Tamai A, Meshi T. 2003. Tomato mosaic virus replication protein suppresses virus-targeted posttranscriptional gene silencing. J. Virol. 77:11016 -11026.
    • (2003) J. Virol. , vol.77 , pp. 11016-11026
    • Kubota, K.1    Tsuda, S.2    Tamai, A.3    Meshi, T.4
  • 25
    • 0347364637 scopus 로고    scopus 로고
    • Systematic, genome-wide identification of host genes affecting replication of a positive-strand RNA virus
    • Kushner DB, et al. 2003. Systematic, genome-wide identification of host genes affecting replication of a positive-strand RNA virus. Proc. Natl. Acad. Sci. U. S. A. 100:15764 -15769.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 15764-15769
    • Kushner, D.B.1
  • 27
    • 33845657428 scopus 로고    scopus 로고
    • UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke
    • Lee JY, Yang W. 2006. UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke. Cell 127:1349 -1360.
    • (2006) Cell , vol.127 , pp. 1349-1360
    • Lee, J.Y.1    Yang, W.2
  • 28
    • 0022273106 scopus 로고
    • 1H-15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type
    • LeMaster DM, Richards FM. 1985. 1H-15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type. Biochemistry 24:7263-7268.
    • (1985) Biochemistry , vol.24 , pp. 7263-7268
    • LeMaster, D.M.1    Richards, F.M.2
  • 29
    • 0030592514 scopus 로고    scopus 로고
    • The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
    • Love RA, et al. 1996. The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site. Cell 87:331-342.
    • (1996) Cell , vol.87 , pp. 331-342
    • Love, R.A.1
  • 30
    • 57149091105 scopus 로고    scopus 로고
    • Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein
    • Luo D, et al. 2008. Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein. EMBO J. 27:3209 -3219.
    • (2008) EMBO J , vol.27 , pp. 3209-3219
    • Luo, D.1
  • 31
    • 0000021646 scopus 로고
    • Two concomitant base substitutions in the putative replicase genes of tobacco mosaic virus confer the ability to overcome the effects of a tomato resistance gene, Tm-1
    • Meshi T, et al. 1988. Two concomitant base substitutions in the putative replicase genes of tobacco mosaic virus confer the ability to overcome the effects of a tomato resistance gene, Tm-1. EMBO J. 7:1575-1581.
    • (1988) EMBO J , vol.7 , pp. 1575-1581
    • Meshi, T.1
  • 32
    • 79954598438 scopus 로고    scopus 로고
    • A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 inmRNAexport
    • Montpetit B, et al. 2011. A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 inmRNAexport. Nature 472:238-242.
    • (2011) Nature , vol.472 , pp. 238-242
    • Montpetit, B.1
  • 33
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris RJ, Perrakis A, Lamzin VS. 2003. ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 374: 229-244.
    • (2003) Methods Enzymol , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 34
    • 84855288767 scopus 로고    scopus 로고
    • A host small GTP-binding protein ARL8 plays crucial roles in Tobamovirus RNA replication
    • doi:10.1371/journal.ppat.1002409
    • Nishikiori M, et al. 2011. A host small GTP-binding protein ARL8 plays crucial roles in Tobamovirus RNA replication. PLoS Pathog. 7:e1002409. doi:10.1371/journal.ppat.1002409.
    • (2011) PLoS Pathog , vol.7
    • Nishikiori, M.1
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Macromol. Crystallogr. A 276:307-326.
    • (1997) Macromol. Crystallogr. A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 13444259748 scopus 로고    scopus 로고
    • Interaction of the tobacco mosaic virus replicase protein with the Aux/IAA protein PAP1/IAA26 is associated with disease development
    • Padmanabhan MS, Goregaoker SP, Golem S, Shiferaw H, Culver JN. 2005. Interaction of the tobacco mosaic virus replicase protein with the Aux/IAA protein PAP1/IAA26 is associated with disease development. J. Virol. 79:2549 -2558.
    • (2005) J. Virol. , vol.79 , pp. 2549-2558
    • Padmanabhan, M.S.1    Goregaoker, S.P.2    Golem, S.3    Shiferaw, H.4    Culver, J.N.5
  • 37
    • 39749169734 scopus 로고    scopus 로고
    • Tobacco mosaic virus replicase-auxin/indole acetic acid protein interactions: reprogramming the auxin response pathway to enhance virus infection
    • Padmanabhan MS, Kramer SR, Wang X, Culver JN. 2008. Tobacco mosaic virus replicase-auxin/indole acetic acid protein interactions: reprogramming the auxin response pathway to enhance virus infection. J. Virol. 82:2477-2485.
    • (2008) J. Virol. , vol.82 , pp. 2477-2485
    • Padmanabhan, M.S.1    Kramer, S.R.2    Wang, X.3    Culver, J.N.4
  • 38
    • 18844455755 scopus 로고    scopus 로고
    • Yeast genome-wide screen reveals dissimilar sets of host genes affecting replication of RNA viruses
    • Panavas T, Serviene E, Brasher J, Nagy PD. 2005. Yeast genome-wide screen reveals dissimilar sets of host genes affecting replication of RNA viruses. Proc. Natl. Acad. Sci. U. S. A. 102:7326 -7331.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 7326-7331
    • Panavas, T.1    Serviene, E.2    Brasher, J.3    Nagy, P.D.4
  • 39
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs
    • Pape T, Schneider TR. 2004. HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs. J. Appl. Crystallogr. 37: 843-844.
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 40
  • 41
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick GM. 2008. A short history of SHELX. Acta Crystallogr. A 64: 112-122.
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 42
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton MR, Dillingham MS, Wigley DB. 2007. Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem. 76:23-50.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 43
    • 0032574840 scopus 로고    scopus 로고
    • A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo
    • Stagljar I, Korostensky C, Johnsson N, te Heesen S. 1998. A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proc. Natl. Acad. Sci. U. S. A. 95:5187-5192.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5187-5192
    • Stagljar, I.1    Korostensky, C.2    Johnsson, N.3    Te Heesen, S.4
  • 44
    • 34247548749 scopus 로고    scopus 로고
    • The double-resistance-breaking Tomato mosaic virus strain ToMV1-2 contains two independent single resistancebreaking domains
    • Strasser M, Pfitzner AJ. 2007. The double-resistance-breaking Tomato mosaic virus strain ToMV1-2 contains two independent single resistancebreaking domains. Arch. Virol. 152:903-914.
    • (2007) Arch. Virol. , vol.152 , pp. 903-914
    • Strasser, M.1    Pfitzner, A.J.2
  • 45
    • 0037439086 scopus 로고    scopus 로고
    • Arabidopsis TOBAMOVIRUS MULTIPLICATION (TOM) 2 locus encodes a transmembrane protein that interacts with TOM1
    • Tsujimoto Y, et al. 2003. Arabidopsis TOBAMOVIRUS MULTIPLICATION (TOM) 2 locus encodes a transmembrane protein that interacts with TOM1. EMBO J. 22:335-343.
    • (2003) EMBO J , vol.22 , pp. 335-343
    • Tsujimoto, Y.1
  • 46
    • 33745184517 scopus 로고    scopus 로고
    • Direct interaction between the tobacco mosaic virus helicase domain and the ATP-bound resistance protein, N factor during the hypersensitive response in tobacco plants
    • Ueda H, Yamaguchi Y, Sano H. 2006. Direct interaction between the tobacco mosaic virus helicase domain and the ATP-bound resistance protein, N factor during the hypersensitive response in tobacco plants. Plant Mol. Biol. 61:31- 45.
    • (2006) Plant Mol. Biol. , vol.61 , pp. 31-45
    • Ueda, H.1    Yamaguchi, Y.2    Sano, H.3
  • 47
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar SS, Soultanas P, Dillingham MS, Subramanya HS, Wigley DB. 1999. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97:75- 84.
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 48
    • 77953025823 scopus 로고    scopus 로고
    • Helicase ATPase activity of the Tobacco mosaic virus 126-kDa protein modulates replicase complex assembly
    • Wang X, Kelman Z, Culver JN. 2010. Helicase ATPase activity of the Tobacco mosaic virus 126-kDa protein modulates replicase complex assembly. Virology 402:292-302.
    • (2010) Virology , vol.402 , pp. 292-302
    • Wang, X.1    Kelman, Z.2    Culver, J.N.3
  • 49
    • 80053633137 scopus 로고    scopus 로고
    • Expression, purification, and functional characterization of a stable helicase domain from a tomato mosaic virus replication protein
    • Xiang H, et al. 2012. Expression, purification, and functional characterization of a stable helicase domain from a tomato mosaic virus replication protein. Protein Expr. Purif. 81:89 -95.
    • (2012) Protein Expr. Purif. , vol.81 , pp. 89-95
    • Xiang, H.1
  • 50
    • 83055169767 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of a helicase-likedomainfromatomatomosaicvirus replication protein
    • Xiang H, et al. 2011. Crystallization and preliminary X-ray crystallographic analysis of a helicase-likedomainfromatomatomosaicvirus replication protein.Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 67:1649-1652.
    • (2011) Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. , vol.67 , pp. 1649-1652
    • Xiang, H.1
  • 51
    • 23244464646 scopus 로고    scopus 로고
    • Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 A
    • Xu T, et al. 2005. Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 A. J. Virol. 79: 10278-10288.
    • (2005) J. Virol. , vol.79 , pp. 10278-10288
    • Xu, T.1
  • 52
    • 0036171919 scopus 로고    scopus 로고
    • Complete inhibition of tobamovirus multiplication by simultaneous mutations in two homologous host genes
    • Yamanaka T, et al. 2002. Complete inhibition of tobamovirus multiplication by simultaneous mutations in two homologous host genes. J. Virol. 76:2491-2497.
    • (2002) J. Virol. , vol.76 , pp. 2491-2497
    • Yamanaka, T.1
  • 53
    • 0034730162 scopus 로고    scopus 로고
    • TOM1, an Arabidopsis gene required for efficient multiplication of a tobamovirus, encodes a putative transmembrane protein
    • Yamanaka T, et al. 2000. TOM1, an Arabidopsis gene required for efficient multiplication of a tobamovirus, encodes a putative transmembrane protein. Proc. Natl. Acad. Sci. U. S. A. 97:10107-10112.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 10107-10112
    • Yamanaka, T.1


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