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Volumn 5, Issue 5, 2010, Pages 873-882

High-stringency tandem affinity purification of proteins conjugated to ubiquitin-like moieties

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; UBIQUITIN;

EID: 77955479945     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2010.40     Document Type: Article
Times cited : (16)

References (46)
  • 2
    • 1342279420 scopus 로고    scopus 로고
    • SUMO and transcriptional regulation. Semin
    • Girdwood, D.W., Tatham, M.H., Hay, R.T. SUMO and transcriptional regulation. Semin. Cell Dev. Biol. 15, 201-210 (2004).
    • (2004) Cell Dev. Biol , vol.15 , pp. 201-210
    • Girdwood, D.W.1    Tatham, M.H.2    Hay, R.T.3
  • 3
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldovan, G.L., Pyrowolakis, G., Jentsch, S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-141 (2002).
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 4
    • 1942437991 scopus 로고    scopus 로고
    • SUMO: A regulator of gene expression and genome integrity
    • Muller, S., Ledl, A., Schmidt, D., SUMO: a regulator of gene expression and genome integrity. Oncogene 23, 1998-2008 (2004).
    • (2004) Oncogene , vol.23 , pp. 1998-2008
    • Muller, S.1    Ledl, A.2    Schmidt, D.3
  • 5
    • 0036300965 scopus 로고    scopus 로고
    • Ubiquitin-related modifier SUMO1
    • Pichler, A., Melchior, F. Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport. Traffic 3, 381-387 (2002).
    • (2002) Traffic , vol.3 , pp. 381-387
    • Pichler, A.1    Melchior, F.2
  • 6
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter, P., Ulrich, H.D. Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature 425, 188-191 (2003).
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 7
    • 33646009148 scopus 로고    scopus 로고
    • Role of ubiquitin-like proteins in transcriptional regulation
    • Hay, R.T. Role of ubiquitin-like proteins in transcriptional regulation. Ernst Schering Res. Found. Workshop 173-192 (2006).
    • (2006) Ernst Schering Res. Found. Workshop , pp. 173-192
    • Hay, R.T.1
  • 8
    • 34248379575 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins in protein regulation
    • Herrmann, J., Lerman, L.O., Lerman, A. Ubiquitin and ubiquitin-like proteins in protein regulation. Circ. Res. 100, 1276-1291 (2007).
    • (2007) Circ. Res , vol.100 , pp. 1276-1291
    • Herrmann, J.1    Lerman, L.O.2    Lerman, A.3
  • 9
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • Jentsch, S., Pyrowolakis, G. Ubiquitin and its kin: how close are the family ties? Trends Cell Biol. 335-342 (2000).
    • (2000) Trends Cell Biol , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 10
    • 63649144413 scopus 로고    scopus 로고
    • Principles of ubiquitin and SUMO modificationsin DNA repair
    • Bergink, S., Jentsch, S. Principles of ubiquitin and SUMO modificationsin DNA repair. Nature 458, 461-467 (2009)
    • (2009) Nature , vol.458 , pp. 461-467
    • Bergink, S.1    Jentsch, S.2
  • 11
    • 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. Mol
    • Tagwerker, C. et al. 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).
    • (2006) Cell Proteomics , vol.5 , pp. 737-748
    • Tagwerker, C.1
  • 12
    • 0342813068 scopus 로고    scopus 로고
    • SUMO-1: Wrestling with a new ubiquitinrelated modifier. Trends Biochem
    • Saitoh, H., Pu, R.T., Dasso, M. SUMO-1: wrestling with a new ubiquitinrelated modifier. Trends Biochem. Sci. 22, 374-376 (1997).
    • (1997) Sci , vol.22 , pp. 374-376
    • Saitoh, H.1    Pu, R.T.2    Dasso, M.3
  • 13
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification. Mol
    • Hay, R.T. SUMO: a history of modification. Mol. Cell 18, 1-12 (2005).
    • (2005) Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 14
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitinrelated protein modifiers SUMO-1 versus SUMO-2/3
    • Saitoh, H., Hinchey, J. Functional heterogeneity of small ubiquitinrelated protein modifiers SUMO-1 versus SUMO-2/3. J. Biol. Chem. 275, 6252-6258 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 15
    • 67649173012 scopus 로고    scopus 로고
    • System-wide changes to SUMO modifications in response to heat shock. Sci. Signal 2
    • Golebiowski, F. et al. System-wide changes to SUMO modifications in response to heat shock. Sci. Signal 2, ra24 (2009).
    • (2009) Ra24
    • Golebiowski, F.1
  • 16
    • 59249102025 scopus 로고    scopus 로고
    • Identification of SUMO target proteins by quantitative proteomics. Methods Mol
    • Andersen, J.S., Matic, I., Vertegaal, A.C. Identification of SUMO target proteins by quantitative proteomics. Methods Mol. Biol. 497, 19-31 (2009).
    • (2009) Biol , vol.497 , pp. 19-31
    • Andersen, J.S.1    Matic, I.2    Vertegaal, A.C.3
  • 17
    • 14644402420 scopus 로고    scopus 로고
    • A universal strategy for proteomic studies of SUMO and other ubiquitinlike modifiers. Mol
    • Rosas-Acosta, G., Russell, W.K., Deyrieux, A., Russell, D.H., Wilson, V.G. A universal strategy for proteomic studies of SUMO and other ubiquitinlike modifiers. mol. Cell Proteomics 4, 56-72(2005).
    • (2005) Cell Proteomics , vol.5672 , pp. 4
    • Rosas-Acosta, G.1    Russell, W.K.2    Deyrieux, A.3    Russell, D.H.4    Wilson, V.G.5
  • 20
    • 26444593473 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry for the analysis of small ubiquitin-like modifier (SUMO) modification: Identification of lysines in RanBP2 and SUMO targeted for modification during the E3 autoSUMOylation reaction. Anal
    • Cooper, H.J. et al. Fourier transform ion cyclotron resonance mass spectrometry for the analysis of small ubiquitin-like modifier (SUMO) modification: identification of lysines in RanBP2 and SUMO targeted for modification during the E3 autoSUMOylation reaction. Anal. Chem. 77, 6310-63(2005).
    • (2005) Chem , vol.77 , pp. 631
    • Cooper, H.J.1
  • 21
    • 33745360876 scopus 로고    scopus 로고
    • Automated identification of SUMOylation sites using mass spectrometry and SUMmOn pattern recognition software. Nat
    • Pedrioli, P.G. et al. Automated identification of SUMOylation sites using mass spectrometry and SUMmOn pattern recognition software. Nat. Methods 3, 533-539 (2006).
    • (2006) Methods , vol.3 , pp. 533-539
    • Pedrioli, P.G.1
  • 22
    • 2442703973 scopus 로고    scopus 로고
    • Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins
    • Zhao, Y., Kwon, S.W., Anselmo, A., Kaur, K., White, M.A. Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins. J. Biol. Chem. 279, 20999-2100(2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 2099
    • Zhao, Y.1    Kwon, S.W.2    Anselmo, A.3    Kaur, K.4    White, M.A.5
  • 23
    • 2942525287 scopus 로고    scopus 로고
    • Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: A proteomic analysis
    • Li, T. et al. Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: a proteomic analysis. Proc. Natl. Acad. Sci. USA 101, 8551-8(2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 101
    • Li, T.1
  • 24
    • 4043051557 scopus 로고    scopus 로고
    • A proteomic study of SUMO-2 target proteins. J. Biol
    • Vertegaal, A.C. et al. A proteomic study of SUMO-2 target proteins. J. Biol. Chem. (2004)
    • (2004) Chem
    • Vertegaal, A.C.1
  • 25
    • 34250155598 scopus 로고    scopus 로고
    • Tandem affinity purification of functional TAP-tagged proteins from human cells. Nat
    • Gregan, J. et al. Tandem affinity purification of functional TAP-tagged proteins from human cells. Nat. Protoc. 2, 1145-1151 (2007).
    • (2007) Protoc , vol.2 , pp. 1145-1151
    • Gregan, J.1
  • 26
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: A general procedure of protein complex purification
    • Puig, O. et al. The tandem affinity purification (TAP) method: a general procedure of protein complex purification. Methods 24, 218-229 (2001).
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1
  • 27
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration. Nat
    • Rigaut, G. et al. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17, 1030-1032 (1999).
    • (1999) Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1
  • 28
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol
    • Desterro, J.M., Rodriguez, M.S., Hay, R.T. SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol. Cell 2, 233-239 (1998).
    • (1998) Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 29
    • 34548178909 scopus 로고    scopus 로고
    • Mann, M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J.V., Mann, M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860 (2006).
    • (2006) Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4
  • 30
    • 34247396011 scopus 로고    scopus 로고
    • A
    • Ong, S.E., Mann, M. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat. Protoc. 1, 2650-2660 (2006).
    • (2006) Protoc , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 31
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC. Nat. Rev
    • Mann, M. Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell Biol. 7, 95(2006).
    • (2006) Mol. Cell Biol , pp. 7-95
    • Mann, M.1
  • 32
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol
    • Ong, S.E. et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell Proteomics 1, 376-386 (2002).
    • (2002) Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1
  • 33
    • 57049091711 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system is a key component of the SUMO-2/3 cycle. Mol
    • Schimmel, J. et al. The ubiquitin-proteasome system is a key component of the SUMO-2/3 cycle. Mol. Cell Proteomics 7, 2107-2122 (2008).
    • (2008) Cell Proteomics , vol.7 , pp. 2107-2122
    • Schimmel, J.1
  • 34
    • 53849109540 scopus 로고    scopus 로고
    • Novel substrates and functions for the ubiquitin-like molecule NEDD8. Biochem
    • Xirodimas, D.P. Novel substrates and functions for the ubiquitin-like molecule NEDD8. Biochem. Soc. Trans. 36, 802-806 (2008).
    • (2008) Soc. Trans , vol.36 , pp. 802-806
    • Xirodimas, D.P.1
  • 35
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis. Nat
    • Wisniewski, J.R., Zougman, A., Nagaraj, N., Mann, M., Universal sample preparation method for proteome analysis. Nat. Methods 6, 359-362 (2009).
    • (2009) Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 36
    • 0036211004 scopus 로고    scopus 로고
    • Protein purification by off-gel electrophoresis
    • Ros, A. et al. Protein purification by off-gel electrophoresis. Proteomics 2, 151-156 (2002).
    • (2002) Proteomics , vol.2 , pp. 151-156
    • Ros, A.1
  • 37
    • 44449108277 scopus 로고    scopus 로고
    • Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry. Nat
    • Nielsen, M.L. et al. Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry. Nat. Methods 5, 459-460 (2008).
    • (2008) Methods , vol.5 , pp. 459-460
    • Nielsen, M.L.1
  • 38
    • 0032544921 scopus 로고    scopus 로고
    • Development of a bicistronic vector driven by the human polypeptide chain elongation factor 1alpha promoter for creation of stable mammalian cell lines that express very high levels of recombinant proteins. Biochem. Biophys. Res
    • Hobbs, S., Jitrapakdee, S., Wallace, J.C. Development of a bicistronic vector driven by the human polypeptide chain elongation factor 1alpha promoter for creation of stable mammalian cell lines that express very high levels of recombinant proteins. Biochem. Biophys. Res. Commun.372 (1998).
    • (1998) Commun , pp. 372
    • Hobbs, S.1    Jitrapakdee, S.2    Wallace, J.C.3
  • 39
    • 58149375807 scopus 로고    scopus 로고
    • Label-free mass spectrometry-based protein quantification technologies in proteomic analysis. Brief Funct
    • Wang, M., You, J., Bemis, K.G., Tegeler, T.J., Brown, D.P. Label-free mass spectrometry-based protein quantification technologies in proteomic analysis. Brief Funct. Genomic Proteomic 7, 329-339 (2008).
    • (2008) Genomic Proteomic , vol.7 , pp. 329-339
    • Wang, M.1    You, J.2    Bemis, K.G.3    Tegeler, T.J.4    Brown, D.P.5
  • 40
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong, S.E., Foster, L.J., Mann, M. Mass spectrometric-based approaches in quantitative proteomics. Methods 29, 124-130 (2003).
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.E.1    Foster, L.J.2    Mann, M.3
  • 41
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative. Nat
    • Ong, S.E., Mann, M. Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 1, 252-262 (2005).
    • (2005) Chem. Biol , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 42
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat
    • Gygi, S.P. et al. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-999 (1999).
    • (1999) Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1
  • 43
    • 33645774852 scopus 로고    scopus 로고
    • Modular stop and go extraction tips with stacked disks for parallel and multidimensional peptide fractionation in proteomics
    • Ishihama, Y., Rappsilber, J., Mann, M. Modular stop and go extraction tips with stacked disks for parallel and multidimensional peptide fractionation in proteomics. J. Proteome Res. 5, 988-994 (2006).
    • (2006) J. Proteome Res , vol.5 , pp. 988-994
    • Ishihama, Y.1    Rappsilber, J.2    Mann, M.3
  • 44
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat
    • Cox, J. et al. A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat. Protoc. 4, 698-705 (2009).
    • (2009) Protoc , vol.4 , pp. 698-705
    • Cox, J.1
  • 45
    • 63049110388 scopus 로고    scopus 로고
    • Mann, M. Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type-specific functions. Mol
    • Pan, C., Kumar, C., Bohl, S., Klingmueller, U., Mann, M. Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type-specific functions. Mol. Cell Proteomics 8, 443-450 (2009).
    • (2009) Cell Proteomics , vol.8 , pp. 443-450
    • Pan, C.1    Kumar, C.2    Bohl, S.3    Klingmueller, U.4
  • 46
    • 41549117597 scopus 로고    scopus 로고
    • Quantitative analysis software tool for mass spectrometry-based proteomics. Nat
    • Park, S.K., Venable, J.D., Xu, T., Yates, J.R.A. III quantitative analysis software tool for mass spectrometry-based proteomics. Nat. Methods 5, 319-322 (2008)
    • (2008) Methods , vol.5 , pp. 319-322
    • Park, S.K.1    Venable, J.D.2    Xu, T.3    Yates, J.4


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