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Volumn 87, Issue 8, 2013, Pages 4704-4715

SCE1, the SUMO-conjugating enzyme in plants that interacts with NIB, the RNA-dependent RNA polymerase of Turnip mosaic virus, is required for viral infection

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; LYSINE; NUCLEAR INCLUSION B PROTEIN; RNA DIRECTED RNA POLYMERASE; SUMO CONJUGATING ENZYME 1; SUMO CONJUGATING ENZYME E2; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 84875784626     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02828-12     Document Type: Article
Times cited : (63)

References (53)
  • 1
    • 33746305530 scopus 로고    scopus 로고
    • Viruses and SUMOylation: recent highlights
    • Boggio R, Chiocca S. 2006. Viruses and SUMOylation: recent highlights. Curr. Opin. Microbiol. 9:430-436.
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 430-436
    • Boggio, R.1    Chiocca, S.2
  • 3
    • 57649198342 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification
    • Zhu J, Zhu S, Guzzo CM, Ellis NA, Sung KS, Choi CY, Matunis MJ. 2008. Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification. J. Biol. Chem. 283:29405-29415.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29405-29415
    • Zhu, J.1    Zhu, S.2    Guzzo, C.M.3    Ellis, N.A.4    Sung, K.S.5    Choi, C.Y.6    Matunis, M.J.7
  • 5
    • 79952335428 scopus 로고    scopus 로고
    • Identification of SUMOylation targets, combined with inactivation of SMT3, reveals the impact of SUMOylation upon growth, morphology, and stress resistance in the pathogen Candida albicans
    • Leach MD, Stead DA, Argo E, Brown AJP. 2011. Identification of SUMOylation targets, combined with inactivation of SMT3, reveals the impact of SUMOylation upon growth, morphology, and stress resistance in the pathogen Candida albicans. Mol. Biol. Cell 22:687-702.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 687-702
    • Leach, M.D.1    Stead, D.A.2    Argo, E.3    Brown, A.J.P.4
  • 6
    • 0033199037 scopus 로고    scopus 로고
    • Isolation of a novelSUMOprotein from tomato that suppresses EIX-induced cell death
    • Hanania U, Furman-Matarasso N, Ron M, Avni A. 1999. Isolation of a novelSUMOprotein from tomato that suppresses EIX-induced cell death. Plant J. 19:533-541.
    • (1999) Plant J. , vol.19 , pp. 533-541
    • Hanania, U.1    Furman-Matarasso, N.2    Ron, M.3    Avni, A.4
  • 7
    • 0142093617 scopus 로고    scopus 로고
    • Xanthomonas type III effector XopD targets SUMO-conjugated protein in planta
    • Hotson A, Chosed R, Shu H, Orth K, Mudgett MB. 2003. Xanthomonas type III effector XopD targets SUMO-conjugated protein in planta. Mol. Microbiol. 50:377-389.
    • (2003) Mol. Microbiol. , vol.50 , pp. 377-389
    • Hotson, A.1    Chosed, R.2    Shu, H.3    Orth, K.4    Mudgett, M.B.5
  • 8
    • 57749115920 scopus 로고    scopus 로고
    • XopD SUMO protease affects host transcription, promotes pathogen growth, and delays symptom development in Xanthomonas-infected tomato leaves
    • Kim JG, Taylor KW, Hotson A, Keegan M, Schmelz EA, Mudgett MB. 2008. XopD SUMO protease affects host transcription, promotes pathogen growth, and delays symptom development in Xanthomonas-infected tomato leaves. Plant Cell 20:1915-1929.
    • (2008) Plant Cell , vol.20 , pp. 1915-1929
    • Kim, J.G.1    Taylor, K.W.2    Hotson, A.3    Keegan, M.4    Schmelz, E.A.5    Mudgett, M.B.6
  • 10
    • 77955898187 scopus 로고    scopus 로고
    • Arabidopsis small ubiquitin-like modifier paralogs have distinct functions in development and defense
    • Van den Burg HA, Kini RK, Schuurink RC, Takken FLW. 2010. Arabidopsis small ubiquitin-like modifier paralogs have distinct functions in development and defense. Plant Cell 22:1998-2016.
    • (2010) Plant Cell , vol.22 , pp. 1998-2016
    • Van den Burg, H.A.1    Kini, R.K.2    Schuurink, R.C.3    Takken, F.L.W.4
  • 11
    • 85016352154 scopus 로고    scopus 로고
    • SUMOylation at the host-pathogen interface
    • Wilson VG. 2012. SUMOylation at the host-pathogen interface. Biomolecules 2:203-227.
    • (2012) Biomolecules , vol.2 , pp. 203-227
    • Wilson, V.G.1
  • 12
    • 0035807718 scopus 로고    scopus 로고
    • Viral interaction with the host cell SUMOylation system
    • Wilson VG, Rangasamy D. 2001. Viral interaction with the host cell SUMOylation system. Virus Res. 81:17-27.
    • (2001) Virus Res. , vol.81 , pp. 17-27
    • Wilson, V.G.1    Rangasamy, D.2
  • 13
    • 84856862707 scopus 로고    scopus 로고
    • Human pathogens and the host cell SUMOylation system
    • Wimmer P, Schreiner S, Dobner T. 2012. Human pathogens and the host cell SUMOylation system. J. Virol. 86:642-654.
    • (2012) J. Virol. , vol.86 , pp. 642-654
    • Wimmer, P.1    Schreiner, S.2    Dobner, T.3
  • 15
    • 0034595239 scopus 로고    scopus 로고
    • Ubiquitin-like proteins: new wines in new bottles
    • Yeh ETH, Gong L, Kamitani T. 2000. Ubiquitin-like proteins: new wines in new bottles. Gene 248:1-14.
    • (2000) Gene , vol.248 , pp. 1-14
    • Yeh, E.T.H.1    Gong, L.2    Kamitani, T.3
  • 16
    • 80052413411 scopus 로고    scopus 로고
    • SUMOylation-promoted enterovirus 71 3C degradation correlates with a reduction in viral replication and cell apoptosis
    • Chen SC, Chang LY, Wang YW, Chen YC, Weng KF, Shih SR, Shih HM. 2011. SUMOylation-promoted enterovirus 71 3C degradation correlates with a reduction in viral replication and cell apoptosis. J. Biol. Chem. 286:31373-31384.
    • (2011) J. Biol. Chem. , vol.286 , pp. 31373-31384
    • Chen, S.C.1    Chang, L.Y.2    Wang, Y.W.3    Chen, Y.C.4    Weng, K.F.5    Shih, S.R.6    Shih, H.M.7
  • 17
    • 77950811209 scopus 로고    scopus 로고
    • SUMOylation of the Epstein-Barr virus BZLF1 protein inhibits its transcriptional activity and is regulated by the virus-encoded protein kinase
    • Hagemeier SR, Dickerson SJ, Meng Q, Yu X, Mertz JE, Kenney SC. 2010. SUMOylation of the Epstein-Barr virus BZLF1 protein inhibits its transcriptional activity and is regulated by the virus-encoded protein kinase. J. Virol. 84:4383-4394.
    • (2010) J. Virol. , vol.84 , pp. 4383-4394
    • Hagemeier, S.R.1    Dickerson, S.J.2    Meng, Q.3    Yu, X.4    Mertz, J.E.5    Kenney, S.C.6
  • 18
    • 0343340071 scopus 로고    scopus 로고
    • Covalent modification of the transactivator protein EI2-p86 of human cytomegalovirus by conjugation to the ubiquitin-homologous proteins SUMO1 and hSMT3b
    • Hofmann H, Floss S, Stamminger T. 2000. Covalent modification of the transactivator protein EI2-p86 of human cytomegalovirus by conjugation to the ubiquitin-homologous proteins SUMO1 and hSMT3b. J. Virol. 74:2510-2524.
    • (2000) J. Virol. , vol.74 , pp. 2510-2524
    • Hofmann, H.1    Floss, S.2    Stamminger, T.3
  • 19
    • 1542317734 scopus 로고    scopus 로고
    • Interaction between a geminivirus replication protein and the plant SUMOylation system
    • Castillo AG, Kong LJ, Hanley-Bowdoin L, Bejarano ER. 2004. Interaction between a geminivirus replication protein and the plant SUMOylation system. J. Virol. 78:2758-2769.
    • (2004) J. Virol. , vol.78 , pp. 2758-2769
    • Castillo, A.G.1    Kong, L.J.2    Hanley-Bowdoin, L.3    Bejarano, E.R.4
  • 23
    • 70349753256 scopus 로고    scopus 로고
    • Turnip mosaic virus RNA replication complex vesicles are mobile, align with microfilaments, and are each derived from a single viral genome
    • Cotton S, Grangeon R, Thivierge K, Mathieu I, Ide C, Wei T, Wang A, Laliberté JF. 2009. Turnip mosaic virus RNA replication complex vesicles are mobile, align with microfilaments, and are each derived from a single viral genome. J. Virol. 83:10460-10471.
    • (2009) J. Virol. , vol.83 , pp. 10460-10471
    • Cotton, S.1    Grangeon, R.2    Thivierge, K.3    Mathieu, I.4    Ide, C.5    Wei, T.6    Wang, A.7    Laliberté, J.F.8
  • 24
    • 77950628398 scopus 로고    scopus 로고
    • Stability of Tobacco etch virus infectious clones in plasmid vectors
    • Bedoya LC, Daros JA. 2010. Stability of Tobacco etch virus infectious clones in plasmid vectors. Virus Res. 149:234-240.
    • (2010) Virus Res. , vol.149 , pp. 234-240
    • Bedoya, L.C.1    Daros, J.A.2
  • 27
    • 77954687469 scopus 로고    scopus 로고
    • Formation of complexes at plasmodesmata for potyvirus intercellular movement is mediated by the viral protein P3N-PIPO
    • doi:10.1371/journal.ppat.1000962
    • Wei T, Zhang C, Hong J, Xiong R, Kasschau KD, Zhou X, Carrington JC, Wang A. 2010. Formation of complexes at plasmodesmata for potyvirus intercellular movement is mediated by the viral protein P3N-PIPO. PLoS Pathog. 6:e1000962. doi:10.1371/journal.ppat.1000962.
    • (2010) PLoS Pathog. , vol.6
    • Wei, T.1    Zhang, C.2    Hong, J.3    Xiong, R.4    Kasschau, K.D.5    Zhou, X.6    Carrington, J.C.7    Wang, A.8
  • 30
    • 78049234670 scopus 로고    scopus 로고
    • Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates identify Arabidopsis proteins implicated in diverse biological processes
    • Elrouby N, Coupland G. 2010. Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates identify Arabidopsis proteins implicated in diverse biological processes. Proc. Natl. Acad. Sci. U. S. A. 107: 17415-17420.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 17415-17420
    • Elrouby, N.1    Coupland, G.2
  • 31
    • 73249148517 scopus 로고    scopus 로고
    • A host RNA helicase-like protein, AtRH8, interacts with the potyviral genome-linked protein, VPg, associates with the virus accumulation complex, and is essential for infection
    • Huang TS, Wei T, Laliberte JF, Wang A. 2010. A host RNA helicase-like protein, AtRH8, interacts with the potyviral genome-linked protein, VPg, associates with the virus accumulation complex, and is essential for infection. Plant Physiol. 152:255-266.
    • (2010) Plant Physiol. , vol.152 , pp. 255-266
    • Huang, T.S.1    Wei, T.2    Laliberte, J.F.3    Wang, A.4
  • 32
    • 0036015061 scopus 로고    scopus 로고
    • Tobacco Rar1, EDS1 and NPR1/NIM1 like genes are required for N-mediated resistance to tobacco mosaic virus
    • Liu Y, Schiff M, Marathe R, Dinesh-Kumar SP. 2002. Tobacco Rar1, EDS1 and NPR1/NIM1 like genes are required for N-mediated resistance to tobacco mosaic virus. Plant J. 30:415-429.
    • (2002) Plant J. , vol.30 , pp. 415-429
    • Liu, Y.1    Schiff, M.2    Marathe, R.3    Dinesh-Kumar, S.P.4
  • 33
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, Zhang Y. 2010. I-TASSER: a unified platform for automated protein structure and function prediction. Nat. Protoc. 5:725-738.
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 34
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • doi:10.1186/1471-2105-9-40
    • Zhang Y. 2008. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9:40. doi:10.1186/1471-2105-9-40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 36
    • 57349168102 scopus 로고    scopus 로고
    • Identification of a movement protein of the Tenuivirus rice stripe virus
    • Xiong R, Wu J, Zhou Y, Zhou X. 2008. Identification of a movement protein of the Tenuivirus rice stripe virus. J. Virol. 82:12304-12311.
    • (2008) J. Virol. , vol.82 , pp. 12304-12311
    • Xiong, R.1    Wu, J.2    Zhou, Y.3    Zhou, X.4
  • 37
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1
    • Bernier-Villamor V, Sampson DA, Matunis MJ, Lima CD. 2002. Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell 108: 345-356.
    • (2002) Cell , vol.108 , pp. 345-356
    • Bernier-Villamor, V.1    Sampson, D.A.2    Matunis, M.J.3    Lima, C.D.4
  • 39
    • 0034730653 scopus 로고    scopus 로고
    • Bovine papillomavirus E1 protein is SUMOylated by the host cell Ubc9 protein
    • Rangasamy D, Wilson VG. 2000. Bovine papillomavirus E1 protein is SUMOylated by the host cell Ubc9 protein. J. Biol. Chem. 275:30487-30495.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30487-30495
    • Rangasamy, D.1    Wilson, V.G.2
  • 40
    • 33750439105 scopus 로고    scopus 로고
    • An extended consensus motif enhances the specificity of substrate modification by SUMO
    • Yang SH, Galanis A, Witty J, Sharrocks AD. 2006. An extended consensus motif enhances the specificity of substrate modification by SUMO. EMBO J. 25:5083-5093.
    • (2006) EMBO J. , vol.25 , pp. 5083-5093
    • Yang, S.H.1    Galanis, A.2    Witty, J.3    Sharrocks, A.D.4
  • 41
    • 34548691835 scopus 로고    scopus 로고
    • Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and SUMO2 to nuclear proteins is essential
    • Saracco SA, Miller MJ, Kurepa J, Vierstra RD. 2007. Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and SUMO2 to nuclear proteins is essential. Plant Physiol. 145:119-134.
    • (2007) Plant Physiol. , vol.145 , pp. 119-134
    • Saracco, S.A.1    Miller, M.J.2    Kurepa, J.3    Vierstra, R.D.4
  • 42
    • 9644278013 scopus 로고    scopus 로고
    • SUMO protein modification
    • Dohmen RJ. 2004. SUMO protein modification. Biochim. Biophys. Acta 1695:113-131.
    • (2004) Biochim. Biophys. Acta , vol.695 , pp. 113-131
    • Dohmen, R.J.1
  • 46
    • 0035949590 scopus 로고    scopus 로고
    • SUMO-1 modification required for transformation by adenovirus type 5 early region 1B 55-kDa oncoprotein
    • Endter C, Kzhyshkowska J, Stauber R, Dobner T. 2001. SUMO-1 modification required for transformation by adenovirus type 5 early region 1B 55-kDa oncoprotein. Proc. Natl. Acad. Sci. U. S. A. 98:11312-11317.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11312-11317
    • Endter, C.1    Kzhyshkowska, J.2    Stauber, R.3    Dobner, T.4
  • 47
    • 0034532450 scopus 로고    scopus 로고
    • SUMO1 modification of bovine papillomavirus E1 protein is required for intranuclear accumulation
    • Rangasamy D, Woytek K, Khan SA, Wilson VG. 2000. SUMO1 modification of bovine papillomavirus E1 protein is required for intranuclear accumulation. J. Biol. Chem. 275:37999-38004.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37999-38004
    • Rangasamy, D.1    Woytek, K.2    Khan, S.A.3    Wilson, V.G.4
  • 48
    • 41649098839 scopus 로고    scopus 로고
    • Heat shock 70 protein interaction with turnip mosaic virus RNA-dependent RNA polymerase within virusinduced membrane vesicles
    • Dufresne PJ, Thivierge K, Cotton S, Beauchemin C, Ide C, Ubalijoro E, Laliberté JF, Fortin MG. 2008. Heat shock 70 protein interaction with turnip mosaic virus RNA-dependent RNA polymerase within virusinduced membrane vesicles. Virology 374:217-227.
    • (2008) Virology , vol.374 , pp. 217-227
    • Dufresne, P.J.1    Thivierge, K.2    Cotton, S.3    Beauchemin, C.4    Ide, C.5    Ubalijoro, E.6    Laliberté, J.F.7    Fortin, M.G.8
  • 49
    • 0006368759 scopus 로고    scopus 로고
    • Functions of the tobacco etch virus RNA polymerase (NIb): subcellular transport and protein-protein interaction with VPg/proteinase (NIa)
    • Li XH, Valdez P, Olvera RE, Carrington JC. 1997. Functions of the tobacco etch virus RNA polymerase (NIb): subcellular transport and protein-protein interaction with VPg/proteinase (NIa). J. Virol. 71:1598-1607.
    • (1997) J. Virol. , vol.71 , pp. 1598-1607
    • Li, X.H.1    Valdez, P.2    Olvera, R.E.3    Carrington, J.C.4
  • 50
    • 44949201423 scopus 로고    scopus 로고
    • Eukaryotic elongation factor 1A interacts with turnip mosaic virus RNA-dependent RNA polymerase and VPg-Pro in virus-induced vesicles
    • Thivierge K, Cotton S, Dufresne PJ, Mathieu I, Beauchemin C, Ide C, Fortin MG, Laliberté JF. 2008. Eukaryotic elongation factor 1A interacts with turnip mosaic virus RNA-dependent RNA polymerase and VPg-Pro in virus-induced vesicles. Virology 377:216-225.
    • (2008) Virology , vol.377 , pp. 216-225
    • Thivierge, K.1    Cotton, S.2    Dufresne, P.J.3    Mathieu, I.4    Beauchemin, C.5    Ide, C.6    Fortin, M.G.7    Laliberté, J.F.8
  • 51
    • 57349162005 scopus 로고    scopus 로고
    • Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmic reticulum exit sites in a COPI-and COPII-dependent manner
    • Wei T, Wang A. 2008. Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmic reticulum exit sites in a COPI-and COPII-dependent manner. J. Virol. 82:12252-12264.
    • (2008) J. Virol. , vol.82 , pp. 12252-12264
    • Wei, T.1    Wang, A.2
  • 53
    • 84866050952 scopus 로고    scopus 로고
    • Ubiquitin and plant viruses, let's play together
    • Alcaide-Loridan C, Jupin I. 2012. Ubiquitin and plant viruses, let's play together. Plant Physiol. 160:72-82.
    • (2012) Plant Physiol. , vol.160 , pp. 72-82
    • Alcaide-Loridan, C.1    Jupin, I.2


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