메뉴 건너뛰기




Volumn 12, Issue 2, 2011, Pages 137-150

The 20S proteasome α5 subunit of Arabidopsis thaliana carries an RNase activity and interacts in planta with the Lettuce mosaic potyvirus HcPro protein

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; CYSTEINE PROTEINASE; GLUTAMIC ACID; GREEN FLUORESCENT PROTEIN; HC PRO PROTEIN, POTYVIRUS; HC-PRO PROTEIN, POTYVIRUS; PAE1 PROTEIN, ARABIDOPSIS; PAE2 PROTEIN, ARABIDOPSIS; PROTEASOME; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; RIBONUCLEASE; VIRUS PROTEIN; VIRUS RNA;

EID: 78650785571     PISSN: 14646722     EISSN: 13643703     Source Type: Journal    
DOI: 10.1111/j.1364-3703.2010.00654.x     Document Type: Article
Times cited : (46)

References (44)
  • 2
    • 0141682702 scopus 로고    scopus 로고
    • Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal [alpha] and [beta] subunits
    • Apcher, G.S., Heink, S., Zantopf, D., Kloetzel, P.-M., Schmid, H.-P., Mayer, R.J. and Kruger, E. (2003) Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal [alpha] and [beta] subunits. FEBS Lett. 553, 200-204.
    • (2003) FEBS Lett. , vol.553 , pp. 200-204
    • Apcher, G.S.1    Heink, S.2    Zantopf, D.3    Kloetzel, P.4    Schmid, H.5    Mayer, R.J.6    Kruger, E.7
  • 5
    • 34548474870 scopus 로고    scopus 로고
    • The Polerovirus silencing suppressor P0 targets ARGONAUTE proteins for degradation
    • Baumberger, N., Tsai, C.H., Lie, M., Havecker, E. and Baulcombe, D.C. (2007) The Polerovirus silencing suppressor P0 targets ARGONAUTE proteins for degradation. Curr. Biol. 17, 1609-1614.
    • (2007) Curr. Biol. , vol.17 , pp. 1609-1614
    • Baumberger, N.1    Tsai, C.H.2    Lie, M.3    Havecker, E.4    Baulcombe, D.C.5
  • 6
    • 0025151515 scopus 로고
    • Potato virus Y helper component protein is associated with amorphous inclusions
    • Baunoch, D.A., Das, P. and Hari, V. (1990) Potato virus Y helper component protein is associated with amorphous inclusions. J. Gen. Virol. 71, 2479-2482.
    • (1990) J. Gen. Virol. , vol.71 , pp. 2479-2482
    • Baunoch, D.A.1    Das, P.2    Hari, V.3
  • 7
    • 0000810989 scopus 로고
    • Altered response to viral infection by tobacco plants perturbed in ubiquitin system
    • Becker, F., Buschfeld, E., Schell, J. and Bachmair, A. (1993) Altered response to viral infection by tobacco plants perturbed in ubiquitin system. Plant J. 3, 875-881.
    • (1993) Plant J. , vol.3 , pp. 875-881
    • Becker, F.1    Buschfeld, E.2    Schell, J.3    Bachmair, A.4
  • 9
    • 0032538794 scopus 로고    scopus 로고
    • Viral pathogenicity determinants are suppressors of transgene silencing in Nicotiana benthamiana
    • Brigneti, G., Voinnet, O., Li, W.X., Ji, L.H., Ding, S.W. and Baulcombe, D.C. (1998) Viral pathogenicity determinants are suppressors of transgene silencing in Nicotiana benthamiana. EMBO J. 17, 6739-6746.
    • (1998) EMBO J. , vol.17 , pp. 6739-6746
    • Brigneti, G.1    Voinnet, O.2    Li, W.X.3    Ji, L.H.4    Ding, S.W.5    Baulcombe, D.C.6
  • 10
    • 75149157140 scopus 로고    scopus 로고
    • The ubiquitin/26S proteasome system in plant-pathogen interactions: a never-ending hide-and-seek game
    • Dielen, A.S., Badaoui, S., Candresse, T. and German-Retana, S. (2010) The ubiquitin/26S proteasome system in plant-pathogen interactions: a never-ending hide-and-seek game. Mol. Plant Pathol. 11, 293-308.
    • (2010) Mol. Plant Pathol. , vol.11 , pp. 293-308
    • Dielen, A.S.1    Badaoui, S.2    Candresse, T.3    German-Retana, S.4
  • 11
    • 34250897234 scopus 로고    scopus 로고
    • Ubiquitin, hormones and biotic stress in plants
    • Dreher, K. and Callis, J. (2007) Ubiquitin, hormones and biotic stress in plants. Ann. Bot. 99, 787-822.
    • (2007) Ann. Bot. , vol.99 , pp. 787-822
    • Dreher, K.1    Callis, J.2
  • 12
    • 0036936858 scopus 로고    scopus 로고
    • Stability in vitro of the 69K movement protein of Turnip yellow mosaic virus is regulated by the ubiquitin-mediated proteasome pathway
    • Drugeon, G. and Jupin, I. (2002) Stability in vitro of the 69K movement protein of Turnip yellow mosaic virus is regulated by the ubiquitin-mediated proteasome pathway. J. Gen. Virol. 83, 3187-3197.
    • (2002) J. Gen. Virol. , vol.83 , pp. 3187-3197
    • Drugeon, G.1    Jupin, I.2
  • 13
    • 0347664051 scopus 로고    scopus 로고
    • The Arabidopsis eukaryotic initiation factor (iso)4E is dispensable for plant growth but required for susceptibility to potyviruses
    • Duprat, A., Caranta, C., Revers, F., Menand, B., Browning, K.S. and Robaglia, C. (2002) The Arabidopsis eukaryotic initiation factor (iso)4E is dispensable for plant growth but required for susceptibility to potyviruses. Plant J. 32, 927-934.
    • (2002) Plant J. , vol.32 , pp. 927-934
    • Duprat, A.1    Caranta, C.2    Revers, F.3    Menand, B.4    Browning, K.S.5    Robaglia, C.6
  • 15
    • 0344196874 scopus 로고    scopus 로고
    • Introduction of a NIa proteinase cleavage site between the reporter gene and HcPro only partially restores the biological properties of GUS- or GFP-tagged LMV
    • German-Retana, S., Redondo, E., Tavert-Roudet, G., Le Gall, O. and Candresse, T. (2003) Introduction of a NIa proteinase cleavage site between the reporter gene and HcPro only partially restores the biological properties of GUS- or GFP-tagged LMV. Virus Res. 98, 151-162.
    • (2003) Virus Res. , vol.98 , pp. 151-162
    • German-Retana, S.1    Redondo, E.2    Tavert-Roudet, G.3    Le Gall, O.4    Candresse, T.5
  • 17
    • 0028253766 scopus 로고
    • Proteasomes (prosomes) inhibit the translation of Tobacco mosaic virus RNA by preventing the formation of initiation complexes
    • Homma, S., Horsch, A., Pouch, M.N., Petit, F., Briand, Y. and Schmid, H.P. (1994) Proteasomes (prosomes) inhibit the translation of Tobacco mosaic virus RNA by preventing the formation of initiation complexes. Mol. Biol. Rep. 20, 57-61.
    • (1994) Mol. Biol. Rep. , vol.20 , pp. 57-61
    • Homma, S.1    Horsch, A.2    Pouch, M.N.3    Petit, F.4    Briand, Y.5    Schmid, H.P.6
  • 18
    • 0033605110 scopus 로고    scopus 로고
    • Possible involvement of proteasomes (prosomes) in AUUUA-mediated mRNA decay
    • Jarrousse, A.-S., Petit, F., Kreutzer-Schmid, C., Gaedigk, R. and Schmid, H.-P. (1999) Possible involvement of proteasomes (prosomes) in AUUUA-mediated mRNA decay. J. Biol. Chem. 274, 5925-5930.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5925-5930
    • Jarrousse, A.1    Petit, F.2    Kreutzer-Schmid, C.3    Gaedigk, R.4    Schmid, H.5
  • 19
    • 36348948068 scopus 로고    scopus 로고
    • HC-Pro protein of Potato virus Y can interact with three Arabidopsis 20S proteasome subunits in planta
    • Jin, Y., Ma, D., Dong, J., Jin, J., Li, D., Deng, C. and Wang, T. (2007) HC-Pro protein of Potato virus Y can interact with three Arabidopsis 20S proteasome subunits in planta. J. Virol. 81, 12 881-12 888.
    • (2007) J. Virol. , vol.81
    • Jin, Y.1    Ma, D.2    Dong, J.3    Jin, J.4    Li, D.5    Deng, C.6    Wang, T.7
  • 20
    • 0033118399 scopus 로고    scopus 로고
    • Proteasome subunit zeta, a putative ribonuclease, is also found as a free monomer
    • Jorgensen, L. and Hendil, K.B. (1999) Proteasome subunit zeta, a putative ribonuclease, is also found as a free monomer. Mol. Biol. Rep. 26, 119-123.
    • (1999) Mol. Biol. Rep. , vol.26 , pp. 119-123
    • Jorgensen, L.1    Hendil, K.B.2
  • 21
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley, L.A. and Sternberg, M.J. (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4, 363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 22
    • 35048903027 scopus 로고    scopus 로고
    • Electron-lucent inclusion bodies are structures specialized for aphid transmission of Cauliflower mosaic virus
    • Khelifa, M., Journou, S., Krishnan, K., Gargani, D., Espérandieu, P., Blanc, S. and Drucker, M. (2007) Electron-lucent inclusion bodies are structures specialized for aphid transmission of Cauliflower mosaic virus. J. Gen. Virol. 88, 2872-2880.
    • (2007) J. Gen. Virol. , vol.88 , pp. 2872-2880
    • Khelifa, M.1    Journou, S.2    Krishnan, K.3    Gargani, D.4    Espérandieu, P.5    Blanc, S.6    Drucker, M.7
  • 24
    • 0000207164 scopus 로고
    • The Plant Viruses 4
    • (Milne, R.G., ed.), New York: Plenum Press.
    • Lesemann, D.E. (1988) Cytopathology. In: The Plant Viruses 4 (Milne, R.G., ed.), pp. 179-227. New York: Plenum Press.
    • (1988) Cytopathology , pp. 179-227
    • Lesemann, D.E.1
  • 25
    • 0035984050 scopus 로고    scopus 로고
    • Role of SCF ubiquitin-ligase and the COP9 signalosome in the N gene-mediated resistance response to Tobacco mosaic virus
    • Liu, Y., Schiff, M., Serino, G., Deng, X.W. and Dinesh-Kumar, S.P. (2002) Role of SCF ubiquitin-ligase and the COP9 signalosome in the N gene-mediated resistance response to Tobacco mosaic virus. Plant Cell, 14, 1483-1496.
    • (2002) Plant Cell , vol.14 , pp. 1483-1496
    • Liu, Y.1    Schiff, M.2    Serino, G.3    Deng, X.W.4    Dinesh-Kumar, S.P.5
  • 31
    • 0029132707 scopus 로고
    • Identification and initial characterization of a specific proteasome (prosome) associated RNase activity
    • Pouch, M.N., Petit, F., Buri, J., Briand, Y. and Schmid, H.P. (1995) Identification and initial characterization of a specific proteasome (prosome) associated RNase activity. J. Biol. Chem. 270, 22 023-22 028.
    • (1995) J. Biol. Chem. , vol.270
    • Pouch, M.N.1    Petit, F.2    Buri, J.3    Briand, Y.4    Schmid, H.P.5
  • 33
    • 0034099838 scopus 로고    scopus 로고
    • Degradation of tobacco mosaic virus movement protein by the 26S proteasome
    • Reichel, C. and Beachy, R.N. (2000) Degradation of tobacco mosaic virus movement protein by the 26S proteasome. J. Virol. 74, 3330-3337.
    • (2000) J. Virol. , vol.74 , pp. 3330-3337
    • Reichel, C.1    Beachy, R.N.2
  • 34
    • 0031742839 scopus 로고    scopus 로고
    • Ultrastructural localization of nonstructural and coat proteins of 19 potyviruses using antisera to bacterially expressed proteins of plum pox virus
    • Riedel, D., Lesemann, D.E. and Maiss, E. (1998) Ultrastructural localization of nonstructural and coat proteins of 19 potyviruses using antisera to bacterially expressed proteins of plum pox virus. Arch. Virol. 143, 2133-2158.
    • (1998) Arch. Virol. , vol.143 , pp. 2133-2158
    • Riedel, D.1    Lesemann, D.E.2    Maiss, E.3
  • 35
    • 0028301965 scopus 로고
    • Loss of a histidine residue at the active site of S-locus ribonuclease is associated with self-compatibility in Lycopersicon peruvianum
    • Royo, J., Kunz, C., Kowyama, Y., Anderson, M., Clarke, A.E. and Nexbigin, E. (1994) Loss of a histidine residue at the active site of S-locus ribonuclease is associated with self-compatibility in Lycopersicon peruvianum. Proc. Natl. Acad. Sci. USA, 91, 6511-6514.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6511-6514
    • Royo, J.1    Kunz, C.2    Kowyama, Y.3    Anderson, M.4    Clarke, A.E.5    Nexbigin, E.6
  • 36
    • 0004255671 scopus 로고
    • The Potyviridae
    • Wallingford, Oxfordshire: CAB International.
    • Shukla, D.D., Ward, C.W. and Brunt, A.A. (1994) The Potyviridae. Wallingford, Oxfordshire: CAB International.
    • (1994)
    • Shukla, D.D.1    Ward, C.W.2    Brunt, A.A.3
  • 37
    • 26044454390 scopus 로고    scopus 로고
    • The tobacco ubiquitin-activating enzymes NtE1A and NtE1B are induced by tobacco mosaic virus, wounding and stress hormones
    • Takizawa, M., Goto, A. and Watanabe, Y. (2005) The tobacco ubiquitin-activating enzymes NtE1A and NtE1B are induced by tobacco mosaic virus, wounding and stress hormones. Mol. Cells, 19, 228-231.
    • (2005) Mol. Cells , vol.19 , pp. 228-231
    • Takizawa, M.1    Goto, A.2    Watanabe, Y.3
  • 38
    • 0024454877 scopus 로고
    • RNA degrading activity is tightly associated with the multicatalytic proteinase, ingensin
    • Tsukahara, T., Tanaka, K., Ogawa, T., Ishiura, S., Funabiki, R. and Sugita, H. (1989) RNA degrading activity is tightly associated with the multicatalytic proteinase, ingensin. FEBS Lett. 255, 179-183.
    • (1989) FEBS Lett. , vol.255 , pp. 179-183
    • Tsukahara, T.1    Tanaka, K.2    Ogawa, T.3    Ishiura, S.4    Funabiki, R.5    Sugita, H.6
  • 39
    • 0036191586 scopus 로고    scopus 로고
    • Structure determination of the constitutive 20S proteasome from bovine liver at 2.75 Å resolution
    • Unno, M., Mizushima, T., Morimoto, Y., Tomisugi, Y., Tanaka, K., Yasuoka, N. and Tsukihara, T. (2002) Structure determination of the constitutive 20S proteasome from bovine liver at 2.75 Å resolution. J. Biochem. 131, 171-173.
    • (2002) J. Biochem. , vol.131 , pp. 171-173
    • Unno, M.1    Mizushima, T.2    Morimoto, Y.3    Tomisugi, Y.4    Tanaka, K.5    Yasuoka, N.6    Tsukihara, T.7
  • 40
    • 0037712997 scopus 로고    scopus 로고
    • The ubiquitin/26S proteasome pathway, the complex last chapter in the life of many plant proteins
    • Vierstra, R.D. (2003) The ubiquitin/26S proteasome pathway, the complex last chapter in the life of many plant proteins. Trends Plant Sci. 8, 135-142.
    • (2003) Trends Plant Sci. , vol.8 , pp. 135-142
    • Vierstra, R.D.1
  • 42
    • 1342346597 scopus 로고    scopus 로고
    • Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms
    • Yang, P., Fu, H., Walker, J., Papa, C.M., Smalle, J., Ju, Y.-M. and Vierstra, R.D. (2004) Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms. J. Biol. Chem. 279, 6401-6413.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6401-6413
    • Yang, P.1    Fu, H.2    Walker, J.3    Papa, C.M.4    Smalle, J.5    Ju, Y.6    Vierstra, R.D.7
  • 43
    • 0033408417 scopus 로고    scopus 로고
    • Alpha5 subunit in Trypanosoma brucei proteasome can self-assemble to form a cylinder of four stacked heptamer rings
    • Yao, Y., Toth, C.R., Huang, L., Wong, M.L., Dias, P., Burlingame, A.L., Coffini, P. and Wang, C.C. (1999) Alpha5 subunit in Trypanosoma brucei proteasome can self-assemble to form a cylinder of four stacked heptamer rings. Biochem. J. 344, 349-358.
    • (1999) Biochem. J. , vol.344 , pp. 349-358
    • Yao, Y.1    Toth, C.R.2    Huang, L.3    Wong, M.L.4    Dias, P.5    Burlingame, A.L.6    Coffini, P.7    Wang, C.C.8
  • 44
    • 0026485797 scopus 로고
    • Role of histidine-40 in ribonuclease T1 catalysis: three-dimensional structures of the partially active His40Lys mutant
    • Zegers, I., Verhelst, P., Choe, H.W., Steyaert, J., Heinemann, U., Saenger, W. and Wyns, L. (1992) Role of histidine-40 in ribonuclease T1 catalysis: three-dimensional structures of the partially active His40Lys mutant. Biochemistry, 31, 11 317-11 325.
    • (1992) Biochemistry , vol.31
    • Zegers, I.1    Verhelst, P.2    Choe, H.W.3    Steyaert, J.4    Heinemann, U.5    Saenger, W.6    Wyns, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.