메뉴 건너뛰기




Volumn 59, Issue 2, 2009, Pages 344-358

Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis

Author keywords

Arabidopsis; Mass spectrometry; Post translation modification; Ubiquitin

Indexed keywords

ARABIDOPSIS PROTEIN; UBIQUITIN;

EID: 67649696034     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2009.03862.x     Document Type: Article
Times cited : (122)

References (60)
  • 1
    • 0025685244 scopus 로고
    • Perturbation of the ubiquitin system causes leaf curling, vascular tissue alterations and necrotic lesions in a higher plant
    • Bachmair, A., Becker, F., Masterson, R.V. Schell, J. (1990) Perturbation of the ubiquitin system causes leaf curling, vascular tissue alterations and necrotic lesions in a higher plant. EMBO J. 9, 4543 4549. (Pubitemid 120026013)
    • (1990) EMBO Journal , vol.9 , Issue.13 , pp. 4543-4549
    • Bachmair, A.1    Becker, F.2    Masterson, R.V.3    Schell, J.4
  • 2
    • 30344460667 scopus 로고    scopus 로고
    • The role of p97/Cdc48p in endoplasmic reticulum-associated degradation: From the immune system to yeast
    • Bar-Nun, S. (2005) The role of p97/Cdc48p in endoplasmic reticulum-associated degradation: from the immune system to yeast. Curr. Top. Microbiol. Immunol. 300, 95 125.
    • (2005) Curr. Top. Microbiol. Immunol. , vol.300 , pp. 95-125
    • Bar-Nun, S.1
  • 3
    • 0000810989 scopus 로고
    • Altered response to viral infection by tobacco plants perturbed in ubiquitin system
    • Becker, F., Buschfeld, E., Schell, J. Bachmair, A. (1993) Altered response to viral infection by tobacco plants perturbed in ubiquitin system. Plant J. 3, 875 881. (Pubitemid 223002677)
    • (1993) Plant Journal , vol.3 , Issue.6 , pp. 875-881
    • Becker, F.1    Buschfeld, E.2    Schell, J.3    Bachmair, A.4
  • 4
    • 34250675590 scopus 로고    scopus 로고
    • The Arabidopsis EIN3 binding F-box proteins EBF1 and EBF2 have distinct but overlapping roles in ethylene signaling
    • DOI 10.1105/tpc.106.048140
    • Binder, B.M., Walker, J.M., Gagne, J.M., Emborg, T.J., Hemmann, G., Bleecker, A.B. Vierstra, R.D. (2007) The Arabidopsis EIN3 binding F-box proteins EBF1 and EBF2 have distinct but overlapping roles in ethylene signaling. Plant Cell, 19, 509 523. (Pubitemid 46941675)
    • (2007) Plant Cell , vol.19 , Issue.2 , pp. 509-523
    • Binder, B.M.1    Walker, J.M.2    Gagne, J.M.3    Emborg, T.J.4    Hemmann, G.5    Bleecker, A.B.6    Vierstra, R.D.7
  • 5
    • 64749095658 scopus 로고    scopus 로고
    • The RPN5 subunit of the 26S proteasome is essential for gametogenesis, sporophyte development, and complex assembly in Arabidopsis
    • Book, A.J., Smalle, J. Lee, K.H., et al. (2009) The RPN5 subunit of the 26S proteasome is essential for gametogenesis, sporophyte development, and complex assembly in Arabidopsis. Plant Cell, 21, 460 478.
    • (2009) Plant Cell , vol.21 , pp. 460-478
    • Book, A.J.1    Smalle, J.2    Lee, K.H.3
  • 6
    • 0028836104 scopus 로고
    • Structure and evolution of genes encoding polyubiquitin and ubiquitin-like proteins in Arabidopsis thaliana ecotype Columbia
    • Callis, J., Carpenter, T., Sun, C.W. Vierstra, R.D. (1995) Structure and evolution of genes encoding polyubiquitin and ubiquitin-like proteins in Arabidopsis thaliana ecotype Columbia. Genetics, 139, 921 939.
    • (1995) Genetics , vol.139 , pp. 921-939
    • Callis, J.1    Carpenter, T.2    Sun, C.W.3    Vierstra, R.D.4
  • 7
    • 16544371166 scopus 로고    scopus 로고
    • Floral dip: Agrobacterium-mediated germ line transformation
    • Clough, S.J. (2005) Floral dip: Agrobacterium-mediated germ line transformation. Methods Mol. Biol. 286, 91 102.
    • (2005) Methods Mol. Biol. , vol.286 , pp. 91-102
    • Clough, S.J.1
  • 8
    • 0033041152 scopus 로고    scopus 로고
    • Sequences within both the N- and C-terminal domains of phytochrome A are required for Pfr ubiquitination and degradation
    • Clough, R.C., Jordan-Beebe, E.T., Lohman, K.N., Marita, J.M., Walker, J.M., Gatz, C. Vierstra, R.D. (1999) Sequences within both the N- and C-terminal domains of phytochrome A are required for Pfr ubiquitination and degradation. Plant J. 17, 155 167.
    • (1999) Plant J. , vol.17 , pp. 155-167
    • Clough, R.C.1    Jordan-Beebe, E.T.2    Lohman, K.N.3    Marita, J.M.4    Walker, J.M.5    Gatz, C.6    Vierstra, R.D.7
  • 9
    • 0003860336 scopus 로고
    • Monoclonal antibodies with differing affinities to the red-absorbing and far-red-absorbing forms of phytochrome
    • Cordonnier, M.M., Greppin, H. Pratt, L.H. (1985) Monoclonal antibodies with differing affinities to the red-absorbing and far-red-absorbing forms of phytochrome. Biochemistry, 24, 3246 3253.
    • (1985) Biochemistry , vol.24 , pp. 3246-3253
    • Cordonnier, M.M.1    Greppin, H.2    Pratt, L.H.3
  • 10
    • 33947712748 scopus 로고    scopus 로고
    • Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry
    • DOI 10.1002/pmic.200600410
    • Denis, N.J., Vasilescu, J., Lambert, J.P., Smith, J.C. Figeys, D. (2007) Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry. Proteomics, 7, 868 874. (Pubitemid 46506734)
    • (2007) Proteomics , vol.7 , Issue.6 , pp. 868-874
    • Denis, N.J.1    Vasilescu, J.2    Lambert, J.-P.3    Smith, J.C.4    Figeys, D.5
  • 11
    • 0034795089 scopus 로고    scopus 로고
    • The ubiquitin-specific protease UBP14 is essential for early embryo development in Arabidopsis thaliana
    • DOI 10.1046/j.1365-313X.2001.01106.x
    • Doelling, J.H., Yan, N., Kurepa, J., Walker, J. Vierstra, R.D. (2001) The ubiquitin-specific protease UBP14 is essential for early embryo development in Arabidopsis thaliana. Plant J. 27, 393 405. (Pubitemid 32943819)
    • (2001) Plant Journal , vol.27 , Issue.5 , pp. 393-405
    • Doelling, J.H.1    Yan, N.2    Kurepa, J.3    Walker, J.4    Vierstra, R.D.5
  • 12
    • 0141567486 scopus 로고    scopus 로고
    • The HECT ubiquitin-protein ligase (UPL) family in Arabidopsis: UPL3 has a specific role in trichome development
    • DOI 10.1046/j.1365-313X.2003.01844.x
    • Downes, B.P., Stupar, R.M., Gingerich, D.J. Vierstra, R.D. (2003) The HECT ubiquitin-protein ligase (UPL) family in Arabidopsis: UPL3 has a specific role in trichome development. Plant J. 35, 729 742. (Pubitemid 37143720)
    • (2003) Plant Journal , vol.35 , Issue.6 , pp. 729-742
    • Downes, B.P.1    Stupar, R.M.2    Gingerich, D.J.3    Vierstra, R.D.4
  • 13
    • 34250897234 scopus 로고    scopus 로고
    • Ubiquitin, hormones and biotic stress in plants
    • DOI 10.1093/aob/mcl255
    • Dreher, K. Callis, J. (2007) Ubiquitin, hormones and biotic stress in plants. Ann. Bot. 99, 787 822. (Pubitemid 47355841)
    • (2007) Annals of Botany , vol.99 , Issue.5 , pp. 787-822
    • Dreher, K.1    Callis, J.2
  • 14
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J.K., McCormack, A.L. Yates, J.R. III. (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976 989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, III.J.R.3
  • 16
    • 34249007126 scopus 로고    scopus 로고
    • A Ubiquitin Stress Response Induces Altered Proteasome Composition
    • DOI 10.1016/j.cell.2007.03.042, PII S009286740700459X
    • Hanna, J., Meides, A., Zhang, D.P. Finley, D. (2007) A ubiquitin stress response induces altered proteasome composition. Cell, 129, 747 759. (Pubitemid 46802382)
    • (2007) Cell , vol.129 , Issue.4 , pp. 747-759
    • Hanna, J.1    Meides, A.2    Zhang, D.P.3    Finley, D.4
  • 17
    • 33646064427 scopus 로고    scopus 로고
    • Structural complexity in ubiquitin recognition
    • Harper, J.W. Schulman, B.A. (2006) Structural complexity in ubiquitin recognition. Cell, 124, 1133 1136.
    • (2006) Cell , vol.124 , pp. 1133-1136
    • Harper, J.W.1    Schulman, B.A.2
  • 19
    • 0033080490 scopus 로고    scopus 로고
    • Use of ubiquitin fusions to augment protein expression in transgenic plants
    • Hondred, D., Walker, J.M., Matthew, D. Vierstra, R.D. (1999) Use of ubiquitin fusions to augment protein expression in transgenic plants. Plant Physiol. 119, 713 724.
    • (1999) Plant Physiol. , vol.119 , pp. 713-724
    • Hondred, D.1    Walker, J.M.2    Matthew, D.3    Vierstra, R.D.4
  • 20
    • 42449119813 scopus 로고    scopus 로고
    • Arabidopsis COP1 shapes the temporal pattern of CO accumulation conferring a photoperiodic flowering response
    • DOI 10.1038/emboj.2008.68, PII EMBOJ200868
    • Jang, S., Marchal, V., Panigrahi, K.C., Wenkel, S., Soppe, W., Deng, X.W., Valverde, F. Coupland, G. (2008) Arabidopsis COP1 shapes the temporal pattern of CO accumulation conferring a photoperiodic flowering response. EMBO J. 27, 1277 1288. (Pubitemid 351574756)
    • (2008) EMBO Journal , vol.27 , Issue.8 , pp. 1277-1288
    • Jang, S.1    Marchal, V.2    Panigrahi, K.C.S.3    Wenkel, S.4    Soppe, W.5    Deng, X.-W.6    Valverde, F.7    Coupland, G.8
  • 22
    • 20044373693 scopus 로고    scopus 로고
    • Proteomic identification of ubiquitinated proteins from human cells expressing His-tagged ubiquitin
    • DOI 10.1002/pmic.200401089
    • Kirkpatrick, D.S., Weldon, S.F., Tsaprailis, G., Liebler, D.C. Gandolfi, A.J. (2005) Proteomic identification of ubiquitinated proteins from human cells expressing His-tagged ubiquitin. Proteomics, 5, 2104 2111. (Pubitemid 40770574)
    • (2005) Proteomics , vol.5 , Issue.8 , pp. 2104-2111
    • Kirkpatrick, D.S.1    Weldon, S.F.2    Tsaprailis, G.3    Liebler, D.C.4    Gandolfi, A.J.5
  • 24
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • DOI 10.1038/ncb1723, PII NCB1723
    • Kraft, C., Deplazes, A., Sohrmann, M. Peter, M. (2008) Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat. Cell Biol. 10, 602 610. (Pubitemid 351627380)
    • (2008) Nature Cell Biology , vol.10 , Issue.5 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 25
    • 0018794827 scopus 로고
    • Synthesis and removal of phenylalanine ammonia-lyase activity in illuminated discs of potato tuber parenchyme
    • Lamb, C.J., Merritt, T.K. Butt, V.S. (1979) Synthesis and removal of phenylalanine ammonia-lyase activity in illuminated discs of potato tuber parenchyme. Biochim. Biophys. Acta, 582, 196 212.
    • (1979) Biochim. Biophys. Acta , vol.582 , pp. 196-212
    • Lamb, C.J.1    Merritt, T.K.2    Butt, V.S.3
  • 26
    • 0034660355 scopus 로고    scopus 로고
    • Histidine-tagged ubiquitin substitutes for wild-type ubiquitin in Saccharomyces cerevisiae and facilitates isolation and identification of in vivo substrates of the ubiquitin pathway
    • DOI 10.1006/abio.2000.4586
    • Ling, R., Colon, E., Dahmus, M.E. Callis, J. (2000) Histidine-tagged ubiquitin substitutes for wild-type ubiquitin in Saccharomyces cerevisiae and facilitates isolation and identification of in vivo substrates of the ubiquitin pathway. Anal. Biochem. 282, 54 64. (Pubitemid 30409424)
    • (2000) Analytical Biochemistry , vol.282 , Issue.1 , pp. 54-64
    • Ling, R.1    Colon, E.2    Dahmus, M.E.3    Callis, J.4
  • 27
    • 34250620427 scopus 로고    scopus 로고
    • The absence of histone H2B monoubiquitination in the Arabidopsis hub1 (rdo4) mutant reveals a role for chromatin remodeling in seed dormancy
    • DOI 10.1105/tpc.106.049221
    • Liu, Y., Koornneef, M. Soppe, W.J. (2007) The absence of histone H2B monoubiquitination in the Arabidopsis hub1 (rdo4) mutant reveals a role for chromatin remodeling in seed dormancy. Plant Cell, 19, 433 444. (Pubitemid 46941669)
    • (2007) Plant Cell , vol.19 , Issue.2 , pp. 433-444
    • Liu, Y.1    Koornneef, M.2    Soppe, W.J.J.3
  • 28
    • 2942620845 scopus 로고    scopus 로고
    • Regulatory mechanisms controlling biogenesis of ubiquitin and the proteasome
    • DOI 10.1016/j.febslet.2004.04.078, PII S001457930400554X
    • London, M.K., Keck, B.I., Ramos, P.C. Dohmen, R.J. (2004) Regulatory mechanisms controlling biogenesis of ubiquitin and the proteasome. FEBS Lett. 567, 259 264. (Pubitemid 38748402)
    • (2004) FEBS Letters , vol.567 , Issue.2-3 , pp. 259-264
    • London, M.K.1    Keck, B.I.2    Ramos, P.C.3    Dohmen, R.J.4
  • 30
    • 34247342702 scopus 로고    scopus 로고
    • Multidimensional protein identification technology (Mud(PIT) analysis of ubiquitinated proteins in plants
    • DOI 10.1074/mcp.M600408-MCP200
    • Maor, R., Jones, A., Nuhse, T.S., Studholme, D.J., Peck, S.C. Shirasu, K. (2007) Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants. Mol. Cell Proteomics, 6, 601 610. (Pubitemid 46630093)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.4 , pp. 601-610
    • Maor, R.1    Jones, A.2    Nuhse, T.S.3    Studholme, D.J.4    Peck, S.C.5    Shirasu, K.6
  • 31
    • 27744500428 scopus 로고    scopus 로고
    • Large-scale analysis of the human ubiquitin-related proteome
    • DOI 10.1002/pmic.200401280
    • Matsumoto, M., Hatakeyama, S., Oyamada, K., Oda, Y., Nishimura, T. Nakayama, K.I. (2005) Large-scale analysis of the human ubiquitin-related proteome. Proteomics, 5, 4145 4151. (Pubitemid 41626082)
    • (2005) Proteomics , vol.5 , Issue.16 , pp. 4145-4151
    • Matsumoto, M.1    Hatakeyama, S.2    Oyamada, K.3    Oda, Y.4    Nishimura, T.5    Nakayama, K.I.6
  • 32
    • 21044460108 scopus 로고    scopus 로고
    • Two-step affinity purification of multiubiquitylated proteins from Saccharomyces cerevisiae
    • DOI 10.1016/S0076-6879(05)99026-5, PII S0076687905990265, 26, Ubiquitin and Protein Degradation, Part B
    • Mayor, T. Deshaies, R.J. (2005) Two-step affinity purification of multiubiquitylated proteins from Saccharomyces cerevisiae. Methods Enzymol. 399, 385 392. (Pubitemid 41772742)
    • (2005) Methods in Enzymology , vol.399 , pp. 385-392
    • Mayor, T.1    Deshaies, R.J.2
  • 33
    • 20444384069 scopus 로고    scopus 로고
    • Analysis of polybiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets
    • DOI 10.1074/mcp.M400220-MCP200
    • Mayor, T., Lipford, J.R., Graumann, J., Smith, G.T. Deshaies, R.J. (2005) Analysis of polyubiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets. Mol. Cell Proteomics, 4, 741 751. (Pubitemid 40873003)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.6 , pp. 741-751
    • Mayor, T.1    Lipford, J.R.2    Graumann, J.3    Smith, G.T.4    Deshaies, R.J.5
  • 34
    • 36749080327 scopus 로고    scopus 로고
    • Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn10 receptor pathway
    • DOI 10.1074/mcp.M700264-MCP200
    • Mayor, T., Graumann, J., Bryan, J., MacCoss, M.J. Deshaies, R.J. (2007) Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn10 receptor pathway. Mol. Cell Proteomics, 6, 1885 1895. (Pubitemid 350201866)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.11 , pp. 1885-1895
    • Mayor, T.1    Graumann, J.2    Bryan, J.3    MacCoss, M.J.4    Deshaies, R.J.5
  • 35
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • DOI 10.1126/science.1127085
    • Mukhopadhyay, D. Riezman, H. (2007) Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science, 315, 201 205. (Pubitemid 46166358)
    • (2007) Science , vol.315 , Issue.5809 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 36
    • 44449108277 scopus 로고    scopus 로고
    • Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry
    • DOI 10.1038/nmeth0608-459, PII NMETH0608-459
    • Nielsen, M.L., Vermeulen, M., Bonaldi, T., Cox, J., Moroder, L. Mann, M. (2008) Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry. Nat. Methods, 5, 459 460. (Pubitemid 351761746)
    • (2008) Nature Methods , vol.5 , Issue.6 , pp. 459-460
    • Nielsen, M.L.1    Vermeulen, M.2    Bonaldi, T.3    Cox, J.4    Moroder, L.5    Mann, M.6
  • 38
    • 0034730745 scopus 로고    scopus 로고
    • Ubiquitin-activating/conjugating activity of TAF(II)250, a mediator of activation of gene expression in Drosophila
    • DOI 10.1126/science.289.5488.2357
    • Pham, A.D. Sauer, F. (2000) Ubiquitin-activating/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila. Science, 289, 2357 2360. (Pubitemid 30739741)
    • (2000) Science , vol.289 , Issue.5488 , pp. 2357-2360
    • Pham, A.-D.1    Sauer, F.2
  • 39
    • 0037646406 scopus 로고    scopus 로고
    • Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains
    • DOI 10.1074/jbc.M212841200
    • Raasi, S. Pickart, C.M. (2003) Rad23 ubiquitin-associated domains (UBA) inhibit 26S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains. J. Biol. Chem. 278, 8951 8959. (Pubitemid 36800372)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.11 , pp. 8951-8959
    • Raasi, S.1    Pickart, C.M.2
  • 40
    • 4143061786 scopus 로고    scopus 로고
    • Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of HHR23A
    • DOI 10.1016/j.jmb.2004.06.057, PII S0022283604007612
    • Raasi, S., Orlov, I., Fleming, K.G. Pickart, C.M. (2004) Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of HHR23A. J. Mol. Biol. 341, 1367 1379. (Pubitemid 39092321)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.5 , pp. 1367-1379
    • Raasi, S.1    Orlov, I.2    Fleming, K.G.3    Pickart, C.M.4
  • 41
    • 33744953644 scopus 로고    scopus 로고
    • Expression of the ubiquitin variant ubR48 decreases proteolytic activity in Arabidopsis and induces cell death
    • DOI 10.1007/s00425-005-0121-z
    • Schlogelhofer, P., Garzon, M., Kerzendorfer, C., Nizhynska, V. Bachmair, A. (2006) Expression of the ubiquitin variant UbR48 decreases proteolytic activity in Arabidopsis and induces cell death. Planta, 223, 684 697. (Pubitemid 43853812)
    • (2006) Planta , vol.223 , Issue.4 , pp. 684-697
    • Schlogelhofer, P.1    Garzon, M.2    Kerzendorfer, C.3    Nizhynska, V.4    Bachmair, A.5
  • 42
    • 44349094727 scopus 로고    scopus 로고
    • Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
    • DOI 10.1038/nature06924, PII NATURE06924
    • Schreiner, P., Chen, X., Husnjak, K., Randles, L., Zhang, N., Elsasser, S., Finley, D., Dikic, I., Walters, K.J. Groll, M. (2008) Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature, 453, 548 552. (Pubitemid 351733316)
    • (2008) Nature , vol.453 , Issue.7194 , pp. 548-552
    • Schreiner, P.1    Chen, X.2    Husnjak, K.3    Randles, L.4    Zhang, N.5    Elsasser, S.6    Finley, D.7    Dikic, I.8    Walters, K.J.9    Groll, M.10
  • 43
    • 3242665372 scopus 로고    scopus 로고
    • The ubiquitin 26S proteasome proteolytic pathway
    • DOI 10.1146/annurev.arplant.55.031903.141801
    • Smalle, J. Vierstra, R.D. (2004) The ubiquitin 26S proteasome proteolytic pathway. Annu. Rev. Plant Biol. 55, 555 590. (Pubitemid 38940944)
    • (2004) Annual Review of Plant Biology , vol.55 , pp. 555-590
    • Smalle, J.1    Vierstra, R.D.2
  • 44
    • 0037390990 scopus 로고    scopus 로고
    • The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis growth and development supports a substrate-specific function in abscisic acid signaling
    • DOI 10.1105/tpc.009217
    • Smalle, J., Kurepa, J., Yang, P., Emborg, T.J., Babiychuk, E., Kushnir, S. Vierstra, R.D. (2003) The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis growth and development supports a substrate-specific function in abscisic acid signaling. Plant Cell, 15, 965 980. (Pubitemid 36453293)
    • (2003) Plant Cell , vol.15 , Issue.4 , pp. 965-980
    • Smalle, J.1    Kurepa, J.2    Yang, P.3    Emborg, T.J.4    Babiychuk, E.5    Kushnir, S.6    Vierstra, R.D.7
  • 45
    • 34250025664 scopus 로고    scopus 로고
    • Control of DNA methylation and heterochromatic silencing by histone H2B deubiquitination
    • DOI 10.1038/nature05864, PII NATURE05864
    • Sridhar, V.V., Kapoor, A., Zhang, K., Zhu, J., Zhou, T., Hasegawa, P.M., Bressan, R.A. Zhu, J.K. (2007) Control of DNA methylation and heterochromatic silencing by histone H2B deubiquitination. Nature, 447, 735 738. (Pubitemid 46889731)
    • (2007) Nature , vol.447 , Issue.7145 , pp. 735-738
    • Sridhar, V.V.1    Kapoor, A.2    Zhang, K.3    Zhu, J.4    Zhou, T.5    Hasegawa, P.M.6    Bressan, R.A.7    Zhu, J.-K.8
  • 46
    • 33947500177 scopus 로고    scopus 로고
    • KEEP ON GOING, a RING E3 ligase essential for Arabidopsis growth and development, is involved in abscisic acid signaling
    • DOI 10.1105/tpc.106.046532
    • Stone, S.L., Williams, L.A., Farmer, L.M., Vierstra, R.D. Callis, J. (2006) KEEP ON GOING, a RING E3 ligase essential for Arabidopsis growth and development, is involved in abscisic acid signaling. Plant Cell, 18, 3415 3428. (Pubitemid 46464902)
    • (2006) Plant Cell , vol.18 , Issue.12 , pp. 3415-3428
    • Stone, S.L.1    Williams, L.A.2    Farmer, L.M.3    Vierstra, R.D.4    Callis, J.5
  • 47
    • 0032794445 scopus 로고    scopus 로고
    • The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast
    • Swaminathan, S., Amerik, A.Y. Hochstrasser, M. (1999) The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast. Mol. Biol. Cell, 10, 2583 2594. (Pubitemid 29393512)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.8 , pp. 2583-2594
    • Swaminathan, S.1    Amerik, A.Y.2    Hochstrasser, M.3
  • 48
    • 33645703441 scopus 로고    scopus 로고
    • A tandem affinity tag for two-step purification under fully denaturing conditions: Application in ubiquitin profiling and protein complex identification combined with in vivo cross-linking
    • Tagwerker, C., Flick, K., Cui, M., Guerrero, C., Dou, Y., Auer, B., Baldi, P., Huang, L. Kaiser, P. (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivo cross-linking. Mol. Cell Proteomics, 5, 737 748.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 737-748
    • Tagwerker, C.1    Flick, K.2    Cui, M.3    Guerrero, C.4    Dou, Y.5    Auer, B.6    Baldi, P.7    Huang, L.8    Kaiser, P.9
  • 49
    • 0027428769 scopus 로고
    • Multiubiquitin chains linked through lysine-48 are abundant in vivo and competent intermediates in the ubiquitin-dependent proteolytic pathway
    • van Nocker, S. Vierstra, R.D. (1993) Multiubiquitin chains linked through lysine-48 are abundant in vivo and competent intermediates in the ubiquitin-dependent proteolytic pathway. J. Biol. Chem. 268, 24766 24773.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24766-24773
    • Van Nocker, S.1    Vierstra, R.D.2
  • 50
    • 0037712997 scopus 로고    scopus 로고
    • The ubiquitin/26S proteasome pathway, the complex last chapter in the life of many plant proteins
    • DOI 10.1016/S1360-1385(03)00014-1
    • 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. (Pubitemid 36726470)
    • (2003) Trends in Plant Science , vol.8 , Issue.3 , pp. 135-142
    • Vierstra, R.D.1
  • 51
    • 67349254570 scopus 로고    scopus 로고
    • The ubiquitin/26S proteasome system at the nexus of plant biology
    • in press).
    • Vierstra, R.D. (2009) The ubiquitin/26S proteasome system at the nexus of plant biology. Nat. Rev. Mol. Cell Biol. (in press).
    • (2009) Nat. Rev. Mol. Cell Biol.
    • Vierstra, R.D.1
  • 52
    • 0023234618 scopus 로고
    • Comparison of the three-dimensional structures of human, yeast, and oat ubiquitin
    • Vijay-Kumar, S., Bugg, C.E., Wilkinson, K.D., Vierstra, R.D., Hatfield, P.M. Cook, W.J. (1987) Comparison of the three-dimensional structures of human, yeast, and oat ubiquitin. J. Biol. Chem. 262, 6396 6399. (Pubitemid 17103051)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.13 , pp. 6396-6399
    • Vijay-Kumar, S.1    Bugg, C.E.2    Wilkinson, K.D.3
  • 53
    • 34147172470 scopus 로고    scopus 로고
    • A ubiquitin-based vector for the co-ordinated synthesis of multiple proteins in plants
    • DOI 10.1111/j.1467-7652.2007.00250.x
    • Walker, J.M. Vierstra, R.D. (2007) Ubiquitin-based vectors for the stoichiometric production of multiple proteins in plants. Plant Biotechnol. J. 5, 413 421. (Pubitemid 46558326)
    • (2007) Plant Biotechnology Journal , vol.5 , Issue.3 , pp. 413-421
    • Walker, J.M.1    Vierstra, R.D.2
  • 54
    • 0036164391 scopus 로고    scopus 로고
    • Antibacterial peptides in stimulated human granulocytes: Characterization of ubiquitinated histone H1A
    • DOI 10.1046/j.0014-2956.2001.02675.x
    • Wang, Y., Griffiths, W.J., Jornvall, H., Agerberth, B. Johansson, J. (2002) Antibacterial peptides in stimulated human granulocytes: characterization of ubiquitinated histone H1A. Eur. J. Biochem. 269, 512 518. (Pubitemid 34128008)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.2 , pp. 512-518
    • Wang, Y.1    Griffiths, W.J.2    Jornvall, H.3    Agerberth, B.4    Johansson, J.5
  • 55
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • DOI 10.1038/85686
    • Washburn, M.P., Wolters, D. Yates, J.R. III. (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19, 242 247. (Pubitemid 32220565)
    • (2001) Nature Biotechnology , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 56
    • 33846488609 scopus 로고    scopus 로고
    • Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue
    • DOI 10.1074/mcp.M00255-MCP200
    • Wisniewski, J.R., Zougman, A., Kruger, S. Mann, M. (2007) Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue. Mol. Cell Proteomics, 6, 72 87. (Pubitemid 46152693)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.1 , pp. 72-87
    • Wisniewski, J.R.1    Zougman, A.2    Kruger, S.3    Mann, M.4
  • 57
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • DOI 10.1021/ac010617e
    • Wolters, D.A., Washburn, M.P. Yates, J.R. III. (2001) An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 73, 5683 5690. (Pubitemid 33126725)
    • (2001) Analytical Chemistry , vol.73 , Issue.23 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 58
    • 0034512691 scopus 로고    scopus 로고
    • The ubiquitin-specific protease family from arabidopsis. AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine
    • DOI 10.1104/pp.124.4.1828
    • Yan, N., Doelling, J.H., Falbel, T.G., Durski, A.M. Vierstra, R.D. (2000) The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine. Plant Physiol. 124, 1828 1843. (Pubitemid 32065166)
    • (2000) Plant Physiology , vol.124 , Issue.4 , pp. 1828-1843
    • Yan, N.1    Doelling, J.H.2    Falbel, T.G.3    Durski, A.M.4    Vierstra, R.D.5
  • 59
    • 1342346597 scopus 로고    scopus 로고
    • Purification of the Arabidopsis 26 S proteasome: Biochemical and molecular analyses revealed the presence of multiple isoforms
    • DOI 10.1074/jbc.M311977200
    • Yang, P., Fu, H., Walker, J., Papa, C.M., Smalle, J., Ju, Y.M. Vierstra, R.D. (2004) Purification of the Arabidopsis 26S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms. J. Biol. Chem. 279, 6401 6413. (Pubitemid 38248774)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 6401-6413
    • Yang, P.1    Fu, H.2    Walker, J.3    Papa, C.M.4    Smalle, J.5    Ju, Y.-M.6    Vierstra, R.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.