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Volumn 174, Issue 1-2, 2011, Pages 158-165

An optimized mRFP-based bimolecular fluorescence complementation system for the detection of protein-protein interactions in planta

Author keywords

Bimolecular fluorescence complementation (BiFC); Capsicum chlorosis virus; Plum pox virus; Protein protein interaction; Red fluorescent protein

Indexed keywords

COAT PROTEIN; MONOMERIC RED FLUORESCENT PROTEIN; PROTEIN BC1; PROTEIN BV1; RED FLUORESCENT PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 79955769528     PISSN: 01660934     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jviromet.2011.03.032     Document Type: Article
Times cited : (21)

References (44)
  • 1
    • 0141789692 scopus 로고    scopus 로고
    • VirE2, a type IV secretion substrate, interacts with the VirD4 transfer protein at cell poles of Agrobacterium tumefaciens
    • Atmakuri K., Ding Z., Christie P.J. VirE2, a type IV secretion substrate, interacts with the VirD4 transfer protein at cell poles of Agrobacterium tumefaciens. Mol. Microbiol. 2003, 49:1699-1713.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1699-1713
    • Atmakuri, K.1    Ding, Z.2    Christie, P.J.3
  • 2
    • 0033516507 scopus 로고    scopus 로고
    • Display of epitopes on the surface of Tobacco mosaic virus: impact of charge and isoelectric point of the epitope on virus-host interactions
    • Bendahmane M., Koo M., Karrer E., Beachy R.N. Display of epitopes on the surface of Tobacco mosaic virus: impact of charge and isoelectric point of the epitope on virus-host interactions. J. Mol. Biol. 1999, 290:9-20.
    • (1999) J. Mol. Biol. , vol.290 , pp. 9-20
    • Bendahmane, M.1    Koo, M.2    Karrer, E.3    Beachy, R.N.4
  • 4
    • 0021771482 scopus 로고
    • Binary Agrobacterium vectors for plant transformation
    • Bevan M. Binary Agrobacterium vectors for plant transformation. Nucleic Acids Res. 1984, 12:8711-8721.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 8711-8721
    • Bevan, M.1
  • 5
    • 33748456465 scopus 로고    scopus 로고
    • The visible touch: in planta visualization of protein-protein interactions by fluorophore-based methods
    • Bhat R.A., Lahaye T., Panstruga R. The visible touch: in planta visualization of protein-protein interactions by fluorophore-based methods. Plant Methods 2006, 2:12.
    • (2006) Plant Methods , vol.2 , pp. 12
    • Bhat, R.A.1    Lahaye, T.2    Panstruga, R.3
  • 6
    • 46049098949 scopus 로고    scopus 로고
    • Transreplication of a Tomato yellow leaf curl Thailand virus DNA-B and replication of a DNA β component by Tomato leaf curl Vietnam virus and Tomato yellow leaf curl Vietnam virus
    • Blawid R., Van D.T., Maiss E. Transreplication of a Tomato yellow leaf curl Thailand virus DNA-B and replication of a DNA β component by Tomato leaf curl Vietnam virus and Tomato yellow leaf curl Vietnam virus. Virus Res. 2008, 136:107-117.
    • (2008) Virus Res. , vol.136 , pp. 107-117
    • Blawid, R.1    Van, D.T.2    Maiss, E.3
  • 8
    • 0023605036 scopus 로고
    • Changes in translational yield regulate tissue-specific expression of beta-glucuronidase
    • Bracey L.T., Paigen K. Changes in translational yield regulate tissue-specific expression of beta-glucuronidase. Proc. Natl. Acad. Sci. U.S.A. 1987, 84:9020-9024.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 9020-9024
    • Bracey, L.T.1    Paigen, K.2
  • 9
    • 7044239645 scopus 로고    scopus 로고
    • Detection of protein-protein interactions in plants using bimolecular fluorescence complementation
    • Bracha-Drori K., Shichrur K., Katz A., Oliva M., Angelovici R., Yalovsky S., Ohad N. Detection of protein-protein interactions in plants using bimolecular fluorescence complementation. Plant J. 2004, 40:419-427.
    • (2004) Plant J. , vol.40 , pp. 419-427
    • Bracha-Drori, K.1    Shichrur, K.2    Katz, A.3    Oliva, M.4    Angelovici, R.5    Yalovsky, S.6    Ohad, N.7
  • 11
    • 38049115791 scopus 로고    scopus 로고
    • Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein-protein interactions in living cells
    • Fan J.Y., Cui Z.-Q., Wei H.-P., Zhang Z.-P., Zhou Y.-F., Wang Y.-P., Zhang X.-E. Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein-protein interactions in living cells. Biochem. Biophys. Res. Commun. 2008, 367:47-53.
    • (2008) Biochem. Biophys. Res. Commun. , vol.367 , pp. 47-53
    • Fan, J.Y.1    Cui, Z.-Q.2    Wei, H.-P.3    Zhang, Z.-P.4    Zhou, Y.-F.5    Wang, Y.-P.6    Zhang, X.-E.7
  • 12
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S., Song O. A novel genetic system to detect protein-protein interactions. Nature 1989, 340:245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 13
    • 11244309033 scopus 로고    scopus 로고
    • Yeast two-hybrid systems confirm the membrane-association and oligomerization of BC1 but do not detect an interaction of the movement proteins BC1 and BV1 of Abutilon mosaic geminivirus
    • Frischmuth S., Kleinow T., Aberle H.-J., Wege C., Hülser D., Jeske H. Yeast two-hybrid systems confirm the membrane-association and oligomerization of BC1 but do not detect an interaction of the movement proteins BC1 and BV1 of Abutilon mosaic geminivirus. Arch. Virol. 2004, 149:2349-2364.
    • (2004) Arch. Virol. , vol.149 , pp. 2349-2364
    • Frischmuth, S.1    Kleinow, T.2    Aberle, H.-J.3    Wege, C.4    Hülser, D.5    Jeske, H.6
  • 14
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • Gordon G.W., Berry G., Liang X.H., Levine B., Herman B. Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys. J. 1998, 74:2702-2713.
    • (1998) Biophys. J. , vol.74 , pp. 2702-2713
    • Gordon, G.W.1    Berry, G.2    Liang, X.H.3    Levine, B.4    Herman, B.5
  • 15
    • 0035057558 scopus 로고    scopus 로고
    • Towards a protein interaction map of potyviruses: protein interaction matrixes of two potyviruses based on the yeast two-hybrid system
    • Guo D., Rajamäki M.L., Saarma M., Valkonen J.P. Towards a protein interaction map of potyviruses: protein interaction matrixes of two potyviruses based on the yeast two-hybrid system. J. Gen. Virol. 2001, 82:935-939.
    • (2001) J. Gen. Virol. , vol.82 , pp. 935-939
    • Guo, D.1    Rajamäki, M.L.2    Saarma, M.3    Valkonen, J.P.4
  • 16
    • 0028500170 scopus 로고
    • The small, versatile pPZP family of Agrobacterium binary vectors for plant transformation
    • Hajdukiewicz P., Svab Z., Maliga P. The small, versatile pPZP family of Agrobacterium binary vectors for plant transformation. Plant Mol. Biol. 1994, 25:989-994.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 989-994
    • Hajdukiewicz, P.1    Svab, Z.2    Maliga, P.3
  • 17
    • 3242701662 scopus 로고    scopus 로고
    • Studying protein-protein interactions via blot overlay or far western blot
    • Hall R.A. Studying protein-protein interactions via blot overlay or far western blot. Methods Mol. Biol. 2004, 261:167-174.
    • (2004) Methods Mol. Biol. , vol.261 , pp. 167-174
    • Hall, R.A.1
  • 18
    • 13644251429 scopus 로고    scopus 로고
    • Use of bimolecular fluorescence complementation to demonstrate transcription factor interaction in nuclei of living cells from the filamentous fungus Acremonium chrysogenum
    • Hoff B., Kück U. Use of bimolecular fluorescence complementation to demonstrate transcription factor interaction in nuclei of living cells from the filamentous fungus Acremonium chrysogenum. Curr. Genet. 2005, 47:132-138.
    • (2005) Curr. Genet. , vol.47 , pp. 132-138
    • Hoff, B.1    Kück, U.2
  • 19
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu C.-D., Chinenov Y., Kerppola T.K. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 2002, 9:789-798.
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.-D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 20
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu C.-D., Kerppola T.K. Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat. Biotechnol. 2003, 21:539-545.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 539-545
    • Hu, C.-D.1    Kerppola, T.K.2
  • 21
    • 33746435428 scopus 로고    scopus 로고
    • An improved mRFP1 adds red to bimolecular fluorescence complementation
    • Jach G., Pesch M., Richter K., Frings S., Uhrig J.F. An improved mRFP1 adds red to bimolecular fluorescence complementation. Nat. Methods 2006, 3:597-600.
    • (2006) Nat. Methods , vol.3 , pp. 597-600
    • Jach, G.1    Pesch, M.2    Richter, K.3    Frings, S.4    Uhrig, J.F.5
  • 22
    • 6344289493 scopus 로고    scopus 로고
    • A protein interaction map of Soybean mosaic virus strain G7H based on the yeast two-hybrid system
    • Kang S.-H., Lim W.-S., Kim K.-H. A protein interaction map of Soybean mosaic virus strain G7H based on the yeast two-hybrid system. Mol. Cells 2004, 18:122-126.
    • (2004) Mol. Cells , vol.18 , pp. 122-126
    • Kang, S.-H.1    Lim, W.-S.2    Kim, K.-H.3
  • 23
    • 30344466668 scopus 로고    scopus 로고
    • Importance of the C-terminal domain of Soybean mosaic virus coat protein for subunit interactions
    • Kang S.-H., Lim W.-S., Hwang S.-H., Park J.-W., Choi H.-S., Kim K.-H. Importance of the C-terminal domain of Soybean mosaic virus coat protein for subunit interactions. J. Gen. Virol. 2006, 87:225-229.
    • (2006) J. Gen. Virol. , vol.87 , pp. 225-229
    • Kang, S.-H.1    Lim, W.-S.2    Hwang, S.-H.3    Park, J.-W.4    Choi, H.-S.5    Kim, K.-H.6
  • 24
    • 34347222583 scopus 로고    scopus 로고
    • Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells
    • Kerppola T.K. Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells. Nat. Protoc. 2006, 1:1278-1286.
    • (2006) Nat. Protoc. , vol.1 , pp. 1278-1286
    • Kerppola, T.K.1
  • 25
    • 35848932556 scopus 로고    scopus 로고
    • New fast BiFC plasmid assay system for in vivo protein-protein interactions
    • Kim M.H., Roh H.E., Lee M.N., Hur M.W. New fast BiFC plasmid assay system for in vivo protein-protein interactions. Cell. Physiol. Biochem. 2007, 20:703-714.
    • (2007) Cell. Physiol. Biochem. , vol.20 , pp. 703-714
    • Kim, M.H.1    Roh, H.E.2    Lee, M.N.3    Hur, M.W.4
  • 26
    • 33747153122 scopus 로고    scopus 로고
    • The complete nucleotide sequence of a Capsicum chlorosis virus isolate from Lycopersicum esculentum in Thailand
    • Knierim D., Blawid R., Maiss E. The complete nucleotide sequence of a Capsicum chlorosis virus isolate from Lycopersicum esculentum in Thailand. Arch. Virol. 2006, 151:1761-1782.
    • (2006) Arch. Virol. , vol.151 , pp. 1761-1782
    • Knierim, D.1    Blawid, R.2    Maiss, E.3
  • 28
    • 0026587042 scopus 로고
    • Infectious in vivo transcripts of a Plum pox potyvirus full-length cDNA clone containing the Cauliflower mosaic virus 35S RNA promoter
    • Maiss E., Timpe U., Brisske-Rode A., Lesemann D.-E., Casper R. Infectious in vivo transcripts of a Plum pox potyvirus full-length cDNA clone containing the Cauliflower mosaic virus 35S RNA promoter. J. Gen. Virol. 1992, 73:709-713.
    • (1992) J. Gen. Virol. , vol.73 , pp. 709-713
    • Maiss, E.1    Timpe, U.2    Brisske-Rode, A.3    Lesemann, D.-E.4    Casper, R.5
  • 29
    • 3242690877 scopus 로고    scopus 로고
    • Co-immunoprecipitation from transfected cells
    • Masters S.C. Co-immunoprecipitation from transfected cells. Methods Mol. Biol. 2004, 261:337-348.
    • (2004) Methods Mol. Biol. , vol.261 , pp. 337-348
    • Masters, S.C.1
  • 30
    • 0024974913 scopus 로고
    • Visualization of protein-nucleic acid interactions in a virus refined structure of intact Tobacco mosaic virus at 2.9Å resolution by X-ray fiber diffraction
    • Namba K., Pattanayek R., Stubbs G. Visualization of protein-nucleic acid interactions in a virus refined structure of intact Tobacco mosaic virus at 2.9Å resolution by X-ray fiber diffraction. J. Mol. Biol. 1989, 208:307-325.
    • (1989) J. Mol. Biol. , vol.208 , pp. 307-325
    • Namba, K.1    Pattanayek, R.2    Stubbs, G.3
  • 31
    • 0028926048 scopus 로고
    • Protein-protein interactions: methods for detection and analysis
    • Phizicky E.M., Fields S. Protein-protein interactions: methods for detection and analysis. Microbiol. Rev. 1995, 59:94-123.
    • (1995) Microbiol. Rev. , vol.59 , pp. 94-123
    • Phizicky, E.M.1    Fields, S.2
  • 32
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa
    • Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal. Biochem. 1987, 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 33
    • 4644349676 scopus 로고    scopus 로고
    • Circular permutation as a tool to reduce surface entropy triggers crystallization of the signal recognition particle receptor beta subunit
    • Schwartz T.U., Walczak R., Blobel G. Circular permutation as a tool to reduce surface entropy triggers crystallization of the signal recognition particle receptor beta subunit. Protein Sci. 2004, 13:2814-2818.
    • (2004) Protein Sci. , vol.13 , pp. 2814-2818
    • Schwartz, T.U.1    Walczak, R.2    Blobel, G.3
  • 34
    • 0037416207 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations
    • Sekar R.B., Periasamy A. Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations. J. Cell Biol. 2003, 160:629-633.
    • (2003) J. Cell Biol. , vol.160 , pp. 629-633
    • Sekar, R.B.1    Periasamy, A.2
  • 35
    • 77952301256 scopus 로고    scopus 로고
    • Protein interaction matrix of Papaya ringspot virus type P based on a yeast two-hybrid system
    • Shen W.T., Wang M.Q., Yan P., Gao L., Zhou P. Protein interaction matrix of Papaya ringspot virus type P based on a yeast two-hybrid system. Acta Virol. 2010, 54:49-54.
    • (2010) Acta Virol. , vol.54 , pp. 49-54
    • Shen, W.T.1    Wang, M.Q.2    Yan, P.3    Gao, L.4    Zhou, P.5
  • 36
    • 14544272790 scopus 로고    scopus 로고
    • The use of fluorescence microscopy to visualise homotypic interactions of tomato spotted wilt virus nucleocapsid protein in living cells
    • Snippe M., Borst J.W., Goldbach R., Kormelink R. The use of fluorescence microscopy to visualise homotypic interactions of tomato spotted wilt virus nucleocapsid protein in living cells. J. Virol. Methods 2005, 125:15-22.
    • (2005) J. Virol. Methods , vol.125 , pp. 15-22
    • Snippe, M.1    Borst, J.W.2    Goldbach, R.3    Kormelink, R.4
  • 37
    • 28444456601 scopus 로고    scopus 로고
    • In planta analysis of protein-protein interactions related to light signaling by bimolecular fluorescence complementation
    • Stolpe T., Süsslin C., Marrocco K., Nick P., Kretsch T., Kircher S. In planta analysis of protein-protein interactions related to light signaling by bimolecular fluorescence complementation. Protoplasma 2005, 226:137-146.
    • (2005) Protoplasma , vol.226 , pp. 137-146
    • Stolpe, T.1    Süsslin, C.2    Marrocco, K.3    Nick, P.4    Kretsch, T.5    Kircher, S.6
  • 38
    • 34548680957 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation analysis system for in vivo detection of protein-protein interaction in Saccharomyces cerevisiae
    • Sung M.-K., Huh W.-K. Bimolecular fluorescence complementation analysis system for in vivo detection of protein-protein interaction in Saccharomyces cerevisiae. Yeast 2007, 24:767-775.
    • (2007) Yeast , vol.24 , pp. 767-775
    • Sung, M.-K.1    Huh, W.-K.2
  • 40
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 1979, 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 41
    • 0033524406 scopus 로고    scopus 로고
    • Homotypic interaction and multimerization of nucleocapsid protein of Tomato spotted wilt tospovirus: identification and characterization of two interacting domains
    • Uhrig J.F., Soellick T.-R., Minke C.J., Philipp Q., Kellmann J.-W., Schreier P.H. Homotypic interaction and multimerization of nucleocapsid protein of Tomato spotted wilt tospovirus: identification and characterization of two interacting domains. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:55-60.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 55-60
    • Uhrig, J.F.1    Soellick, T.-R.2    Minke, C.J.3    Philipp, Q.4    Kellmann, J.-W.5    Schreier, P.H.6
  • 42
    • 0037342553 scopus 로고    scopus 로고
    • An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of Tomato bushy stunt virus
    • Voinnet O., Rivas S., Mestre P., Baulcombe D. An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of Tomato bushy stunt virus. Plant J. 2003, 33:949-956.
    • (2003) Plant J. , vol.33 , pp. 949-956
    • Voinnet, O.1    Rivas, S.2    Mestre, P.3    Baulcombe, D.4


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