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Volumn 69, Issue 7, 2012, Pages 1025-1033

GFP tagging sheds light on protein translocation: Implications for key methods in cell biology

Author keywords

GFP tagging; Green fluorescent protein; Protein localization; Protein translocase; Protein transport machineries

Indexed keywords

GREEN FLUORESCENT PROTEIN; MITOCHONDRIAL PROTEIN; PROTEIN TIM23; PROTEIN TOM; UNCLASSIFIED DRUG;

EID: 84859156448     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-0932-6     Document Type: Article
Times cited : (6)

References (53)
  • 1
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien RY (1998) The green fluorescent protein. Annu Rev Biochem 67:509-544
    • (1998) Annu Rev Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 2
    • 0036489443 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP): Applications, structure, and related photophysical behavior
    • Zimmer M (2002) Green fluorescent protein (GFP): applications, structure, and related photophysical behavior. Chem Rev 102(3):759-781
    • (2002) Chem Rev , vol.102 , Issue.3 , pp. 759-781
    • Zimmer, M.1
  • 3
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • Giepmans BN, Adams SR, Ellisman MH, Tsien RY (2006) The fluorescent toolbox for assessing protein location and function. Science 312(5771):217-224
    • (2006) Science , vol.312 , Issue.5771 , pp. 217-224
    • Giepmans, B.N.1    Adams, S.R.2    Ellisman, M.H.3    Tsien, R.Y.4
  • 4
    • 0032499784 scopus 로고    scopus 로고
    • Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins
    • Llopis J, McCaffery JM, Miyawaki A, Farquhar MG, Tsien RY (1998) Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc Natl Acad Sci USA 95(12):6803-6808
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.12 , pp. 6803-6808
    • Llopis, J.1    McCaffery, J.M.2    Miyawaki, A.3    Farquhar, M.G.4    Tsien, R.Y.5
  • 5
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis
    • Matsuyama S, Llopis J, Deveraux QL, Tsien RY, Reed JC (2000) Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis. Nat Cell Biol 2(6):318-325
    • (2000) Nat Cell Biol , vol.2 , Issue.6 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 6
    • 33646677239 scopus 로고    scopus 로고
    • Measuring intracellular redox conditions using GFP-based sensors
    • Bjornberg O, Ostergaard H, Winther JR (2006) Measuring intracellular redox conditions using GFP-based sensors. Antioxid Redox Signal 8(3-4):354-361
    • (2006) Antioxid Redox Signal , vol.8 , Issue.3-4 , pp. 354-361
    • Bjornberg, O.1    Ostergaard, H.2    Winther, J.R.3
  • 8
    • 77954356493 scopus 로고    scopus 로고
    • Fluorescent protein-based redox probes
    • Meyer AJ, Dick TP (2010) Fluorescent protein-based redox probes. Antioxid Redox Signal 13(5):621-650
    • (2010) Antioxid Redox Signal , vol.13 , Issue.5 , pp. 621-650
    • Meyer, A.J.1    Dick, T.P.2
  • 9
    • 0035502932 scopus 로고    scopus 로고
    • Shedding light on disulfide bond formation: Engineering a redox switch in green fluorescent protein
    • Ostergaard H, Henriksen A, Hansen FG, Winther JR (2001) Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein. EMBO J 20(21):5853-5862
    • (2001) EMBO J , vol.20 , Issue.21 , pp. 5853-5862
    • Ostergaard, H.1    Henriksen, A.2    Hansen, F.G.3    Winther, J.R.4
  • 10
    • 70349318573 scopus 로고    scopus 로고
    • Green fluorescent protein: Structure, folding and chromophore maturation
    • Craggs TD (2009) Green fluorescent protein: structure, folding and chromophore maturation. Chem Soc Rev 38(10):2865-2875
    • (2009) Chem Soc Rev , vol.38 , Issue.10 , pp. 2865-2875
    • Craggs, T.D.1
  • 11
    • 0031006611 scopus 로고    scopus 로고
    • Chromophore formation in green fluorescent protein
    • Reid BG, Flynn GC (1997) Chromophore formation in green fluorescent protein. Biochemistry 36(22):6786-6791
    • (1997) Biochemistry , vol.36 , Issue.22 , pp. 6786-6791
    • Reid, B.G.1    Flynn, G.C.2
  • 12
    • 0034601826 scopus 로고    scopus 로고
    • Folding of green fluorescent protein and the cycle3 mutant
    • Fukuda H, Arai M, Kuwajima K (2000) Folding of green fluorescent protein and the cycle3 mutant. Biochemistry 39(39): 12025-12032
    • (2000) Biochemistry , vol.39 , Issue.39 , pp. 12025-12032
    • Fukuda, H.1    Arai, M.2    Kuwajima, K.3
  • 13
    • 70349328442 scopus 로고    scopus 로고
    • The folding, stability and conformational dynamics of beta-barrel fluorescent proteins
    • Hsu ST, Blaser G, Jackson SE (2009) The folding, stability and conformational dynamics of beta-barrel fluorescent proteins. Chem Soc Rev 38(10):2951-2965
    • (2009) Chem Soc Rev , vol.38 , Issue.10 , pp. 2951-2965
    • Hsu, S.T.1    Blaser, G.2    Jackson, S.E.3
  • 14
    • 80155192450 scopus 로고    scopus 로고
    • Lateral release of proteins from the TOM complex into the outer membrane of mitochondria
    • Harner M, Neupert W, Deponte M (2011) Lateral release of proteins from the TOM complex into the outer membrane of mitochondria. EMBO J 30(16):3232-3241
    • (2011) EMBO J , vol.30 , Issue.16 , pp. 3232-3241
    • Harner, M.1    Neupert, W.2    Deponte, M.3
  • 15
    • 79959435716 scopus 로고    scopus 로고
    • Assembly of bacterial inner membrane proteins
    • Dalbey RE, Wang P, Kuhn A (2011) Assembly of bacterial inner membrane proteins. Annu Rev Biochem 80:161-187
    • (2011) Annu Rev Biochem , vol.80 , pp. 161-187
    • Dalbey, R.E.1    Wang, P.2    Kuhn, A.3
  • 17
    • 79851514906 scopus 로고    scopus 로고
    • Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria
    • Robinson C, Matos CF, Beck D, Ren C, Lawrence J, Vasisht N, Mendel S (2011) Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria. Biochim Biophys Acta 1808(3):876-884
    • (2011) Biochim Biophys Acta , vol.1808 , Issue.3 , pp. 876-884
    • Robinson, C.1    Matos, C.F.2    Beck, D.3    Ren, C.4    Lawrence, J.5    Vasisht, N.6    Mendel, S.7
  • 18
    • 78651367836 scopus 로고    scopus 로고
    • Evolution of YidC/Oxa1/Alb3 insertases: Three independent gene duplications followed by functional specialization in bacteria, mitochondria and chloroplasts
    • Funes S, Kauff F, van der Sluis EO, Ott M, Herrmann JM (2011) Evolution of YidC/Oxa1/Alb3 insertases: three independent gene duplications followed by functional specialization in bacteria, mitochondria and chloroplasts. Biol Chem 392(1-2):13-19
    • (2011) Biol Chem , vol.392 , Issue.1-2 , pp. 13-19
    • Funes, S.1    Kauff, F.2    Van Der Sluis, E.O.3    Ott, M.4    Herrmann, J.M.5
  • 19
    • 79959468179 scopus 로고    scopus 로고
    • B-Barrel membrane protein assembly by the Bam complex
    • Hagan CL, Silhavy TJ, Kahne D (2011) b-Barrel membrane protein assembly by the Bam complex. Annu Rev Biochem 80:189-210
    • (2011) Annu Rev Biochem , vol.80 , pp. 189-210
    • Hagan, C.L.1    Silhavy, T.J.2    Kahne, D.3
  • 20
    • 79851513761 scopus 로고    scopus 로고
    • Multiple pathways in the integration of proteins into the mitochondrial outer membrane
    • Dukanovic J, Rapaport D (2011) Multiple pathways in the integration of proteins into the mitochondrial outer membrane. Biochim Biophys Acta 1808(3):971-980
    • (2011) Biochim Biophys Acta , vol.1808 , Issue.3 , pp. 971-980
    • Dukanovic, J.1    Rapaport, D.2
  • 22
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: Machineries and mechanisms
    • Chacinska A, Koehler CM, Milenkovic D, Lithgow T, Pfanner N (2009) Importing mitochondrial proteins: machineries and mechanisms. Cell 138(4):628-644
    • (2009) Cell , vol.138 , Issue.4 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 23
    • 70349451660 scopus 로고    scopus 로고
    • Multiple pathways for mitochondrial protein traffic
    • Endo T, Yamano K (2009) Multiple pathways for mitochondrial protein traffic. Biol Chem 390(8):723-730
    • (2009) Biol Chem , vol.390 , Issue.8 , pp. 723-730
    • Endo, T.1    Yamano, K.2
  • 24
    • 78650517733 scopus 로고    scopus 로고
    • Common ground for protein translocation: Access control for mitochondria and chloroplasts
    • Schleiff E, Becker T (2011) Common ground for protein translocation: access control for mitochondria and chloroplasts. Natl Rev Mol Cell Biol 12(1):48-59
    • (2011) Natl Rev Mol Cell Biol , vol.12 , Issue.1 , pp. 48-59
    • Schleiff, E.1    Becker, T.2
  • 27
  • 28
    • 60049091769 scopus 로고    scopus 로고
    • ESX/type VII secretion systems and their role in host-pathogen interaction
    • Simeone R, Bottai D, Brosch R (2009) ESX/type VII secretion systems and their role in host-pathogen interaction. Curr Opin Microbiol 12(1):4-10
    • (2009) Curr Opin Microbiol , vol.12 , Issue.1 , pp. 4-10
    • Simeone, R.1    Bottai, D.2    Brosch, R.3
  • 31
    • 33750305666 scopus 로고    scopus 로고
    • Dynamic subcompartmentalization of the mitochondrial inner membrane
    • Vogel F, Bornhovd C, Neupert W, Reichert AS (2006) Dynamic subcompartmentalization of the mitochondrial inner membrane. J Cell Biol 175(2):237-247
    • (2006) J Cell Biol , vol.175 , Issue.2 , pp. 237-247
    • Vogel, F.1    Bornhovd, C.2    Neupert, W.3    Reichert, A.S.4
  • 32
    • 27744543167 scopus 로고    scopus 로고
    • How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?
    • Rapaport D (2005) How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane? J Cell Biol 171(3):419-423
    • (2005) J Cell Biol , vol.171 , Issue.3 , pp. 419-423
    • Rapaport, D.1
  • 33
    • 79960716413 scopus 로고    scopus 로고
    • Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation
    • Karbowski M, Youle RJ (2011) Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation. Curr Opin Cell Biol 23(4):476-482
    • (2011) Curr Opin Cell Biol , vol.23 , Issue.4 , pp. 476-482
    • Karbowski, M.1    Youle, R.J.2
  • 34
    • 62649094413 scopus 로고    scopus 로고
    • Transmembrane passage of hydrophobic compounds through a protein channel wall
    • Hearn EM, Patel DR, Lepore BW, Indic M, van den Berg B (2009) Transmembrane passage of hydrophobic compounds through a protein channel wall. Nature 458(7236):367-370
    • (2009) Nature , vol.458 , Issue.7236 , pp. 367-370
    • Hearn, E.M.1    Patel, D.R.2    Lepore, B.W.3    Indic, M.4    Van Den Berg, B.5
  • 35
    • 44349105790 scopus 로고    scopus 로고
    • Active remodelling of the TIM23 complex during translocation of preproteins into mitochondria
    • Popov-Celeketic D, Mapa K, Neupert W, Mokranjac D (2008) Active remodelling of the TIM23 complex during translocation of preproteins into mitochondria. EMBO J 27(10):1469-1480
    • (2008) EMBO J , vol.27 , Issue.10 , pp. 1469-1480
    • Popov-Celeketic, D.1    Mapa, K.2    Neupert, W.3    Mokranjac, D.4
  • 36
    • 0142105410 scopus 로고    scopus 로고
    • Mitochondrial translocation contact sites: Separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex
    • Chacinska A, Rehling P, Guiard B, Frazier AE, Schulze-Specking A, Pfanner N, Voos W, Meisinger C (2003) Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex. EMBO J 22(20):5370-5381
    • (2003) EMBO J , vol.22 , Issue.20 , pp. 5370-5381
    • Chacinska, A.1    Rehling, P.2    Guiard, B.3    Frazier, A.E.4    Schulze-Specking, A.5    Pfanner, N.6    Voos, W.7    Meisinger, C.8
  • 38
    • 0031969732 scopus 로고    scopus 로고
    • Identification of the protein import components of the rat mitochondrial inner membrane, rTIM17, rTIM23, and rTIM44
    • Ishihara N, Mihara K (1998) Identification of the protein import components of the rat mitochondrial inner membrane, rTIM17, rTIM23, and rTIM44. J Biochem 123(4):722-732
    • (1998) J Biochem , vol.123 , Issue.4 , pp. 722-732
    • Ishihara, N.1    Mihara, K.2
  • 40
    • 0037393286 scopus 로고    scopus 로고
    • Identification, expression, and import of components 17 and 23 of the inner mitochondrial membrane translocase from Arabidopsis
    • Murcha MW, Lister R, Ho AY, Whelan J (2003) Identification, expression, and import of components 17 and 23 of the inner mitochondrial membrane translocase from Arabidopsis. Plant Physiol 131(4):1737-1747
    • (2003) Plant Physiol , vol.131 , Issue.4 , pp. 1737-1747
    • Murcha, M.W.1    Lister, R.2    Ho, A.Y.3    Whelan, J.4
  • 41
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • doi:10.1038/322228a0
    • Eilers M, Schatz G (1986) Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature 322(6076):228-232. doi:10.1038/322228a0
    • (1986) Nature , vol.322 , Issue.6076 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 42
    • 0023989329 scopus 로고
    • Unfolding and refolding of a purified precursor protein during import into isolated mitochondria
    • Eilers M, Hwang S, Schatz G (1988) Unfolding and refolding of a purified precursor protein during import into isolated mitochondria. EMBO J 7(4):1139-1145
    • (1988) EMBO J , vol.7 , Issue.4 , pp. 1139-1145
    • Eilers, M.1    Hwang, S.2    Schatz, G.3
  • 43
    • 0024454311 scopus 로고
    • Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites
    • Rassow J, Guiard B, Wienhues U, Herzog V, Hartl FU, Neupert W (1989) Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites. J Cell Biol 109(4 Pt 1):1421-1428
    • (1989) J Cell Biol , vol.109 , Issue.4 PART 1 , pp. 1421-1428
    • Rassow, J.1    Guiard, B.2    Wienhues, U.3    Herzog, V.4    Hartl, F.U.5    Neupert, W.6
  • 44
    • 0023656946 scopus 로고
    • The role of protein structure in the mitochondrial import pathway. Unfolding of mitochondrially bound precursors is required for membrane translocation
    • Chen WJ, Douglas MG (1987) The role of protein structure in the mitochondrial import pathway. Unfolding of mitochondrially bound precursors is required for membrane translocation. J Biol Chem 262(32):15605-15609
    • (1987) J Biol Chem , vol.262 , Issue.32 , pp. 15605-15609
    • Chen, W.J.1    Douglas, M.G.2
  • 45
    • 0028859492 scopus 로고
    • Avidin fusion protein as a tool to generate a stable translocation intermediate spanning the mitochondrial membranes
    • Endo T, Nakayama Y, Nakai M (1995) Avidin fusion protein as a tool to generate a stable translocation intermediate spanning the mitochondrial membranes. J Biochem 118(4):753-759
    • (1995) J Biochem , vol.118 , Issue.4 , pp. 753-759
    • Endo, T.1    Nakayama, Y.2    Nakai, M.3
  • 46
    • 0033529681 scopus 로고    scopus 로고
    • A multisubunit complex of outer and inner mitochondrial membrane protein translocases stabilized in vivo by translocation intermediates
    • Schulke N, Sepuri NB, Gordon DM, Saxena S, Dancis A, Pain D (1999) A multisubunit complex of outer and inner mitochondrial membrane protein translocases stabilized in vivo by translocation intermediates. J Biol Chem 274(32):22847-22854
    • (1999) J Biol Chem , vol.274 , Issue.32 , pp. 22847-22854
    • Schulke, N.1    Sepuri, N.B.2    Gordon, D.M.3    Saxena, S.4    Dancis, A.5    Pain, D.6
  • 47
    • 0030787527 scopus 로고    scopus 로고
    • In vivo zippering of inner and outer mitochondrial membranes by a stable translocation intermediate
    • Schulke N, Sepuri NB, Pain D (1997) In vivo zippering of inner and outer mitochondrial membranes by a stable translocation intermediate. Proc Natl Acad Sci USA 94(14):7314-7319
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.14 , pp. 7314-7319
    • Schulke, N.1    Sepuri, N.B.2    Pain, D.3
  • 48
    • 0024202929 scopus 로고
    • A chimeric mitochondrial precursor protein with internal disulfide bridges blocks import of
    • authentic precursors into mitochondria and allows quantitation of import sites
    • Vestweber D, Schatz G (1988) A chimeric mitochondrial precursor protein with internal disulfide bridges blocks import of authentic precursors into mitochondria and allows quantitation of import sites. J Cell Biol 107(6 Pt 1):2037-2043
    • (1988) J Cell Biol , vol.107 , Issue.6 PART 1 , pp. 2037-2043
    • Vestweber, D.1    Schatz, G.2
  • 49
    • 57349134513 scopus 로고    scopus 로고
    • Engineering a novel multifunctional green fluorescent protein tag for a wide variety of protein research
    • Kobayashi T, Morone N, Kashiyama T, Oyamada H, Kurebayashi N, Murayama T (2008) Engineering a novel multifunctional green fluorescent protein tag for a wide variety of protein research. PLoS One 3(12):e3822
    • (2008) PLoS One , vol.3 , Issue.12
    • Kobayashi, T.1    Morone, N.2    Kashiyama, T.3    Oyamada, H.4    Kurebayashi, N.5    Murayama, T.6
  • 50
    • 40849119674 scopus 로고    scopus 로고
    • Purification of GFP fusion proteins with high purity and yield by monoclonal antibody-coupled affinity column chromatography
    • Zhuang R, Zhang Y, Zhang R, Song C, Yang K, Yang A, Jin B (2008) Purification of GFP fusion proteins with high purity and yield by monoclonal antibody-coupled affinity column chromatography. Protein Expr Purif 59(1):138-143
    • (2008) Protein Expr Purif , vol.59 , Issue.1 , pp. 138-143
    • Zhuang, R.1    Zhang, Y.2    Zhang, R.3    Song, C.4    Yang, K.5    Yang, A.6    Jin, B.7


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