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Volumn 7, Issue 8, 2012, Pages

Nuclear import and dimerization of tomato ASR1, a water stress-inducible protein exclusive to plants

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DIMER; HOMODIMER; LYSINE; PROTEIN ASR1; UNCLASSIFIED DRUG;

EID: 84865013135     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0041008     Document Type: Article
Times cited : (28)

References (33)
  • 1
    • 0027639774 scopus 로고
    • Tomato (Lycopersicon esculentum) transcript induced by water deficit and ripening
    • Iusem ND, Bartholomew DM, Hitz WD, Scolnik PA, (1993) Tomato (Lycopersicon esculentum) transcript induced by water deficit and ripening. Plant Physiol 102: 1353-1354.
    • (1993) Plant Physiol , vol.102 , pp. 1353-1354
    • Iusem, N.D.1    Bartholomew, D.M.2    Hitz, W.D.3    Scolnik, P.A.4
  • 2
    • 0346095402 scopus 로고    scopus 로고
    • Adaptive evolution of the water stress-induced gene Asr2 in Lycopersicon species dwelling in arid habitats
    • Frankel N, Hasson E, Iusem ND, Rossi MS, (2003) Adaptive evolution of the water stress-induced gene Asr2 in Lycopersicon species dwelling in arid habitats. Mol Biol Evol 20: 1955-1962.
    • (2003) Mol Biol Evol , vol.20 , pp. 1955-1962
    • Frankel, N.1    Hasson, E.2    Iusem, N.D.3    Rossi, M.S.4
  • 3
    • 33746488455 scopus 로고    scopus 로고
    • Evolutionary history of the Asr gene family
    • Frankel N, Carrari F, Hasson E, Iusem ND, (2006) Evolutionary history of the Asr gene family. Gene 378: 74-83.
    • (2006) Gene , vol.378 , pp. 74-83
    • Frankel, N.1    Carrari, F.2    Hasson, E.3    Iusem, N.D.4
  • 5
    • 42149185104 scopus 로고    scopus 로고
    • Synergism between the chaperone-like activity of the stress regulated ASR1 protein and the osmolyte glycine-betaine
    • Konrad Z, Bar-Zvi D, (2008) Synergism between the chaperone-like activity of the stress regulated ASR1 protein and the osmolyte glycine-betaine. Planta 227: 1213-1219.
    • (2008) Planta , vol.227 , pp. 1213-1219
    • Konrad, Z.1    Bar-Zvi, D.2
  • 6
    • 33847320155 scopus 로고    scopus 로고
    • ci21A/Asr1 expression influences glucose accumulation in potato tubers
    • Frankel N, Nunes-Nesi A, Balbo I, Mazuch J, Centeno D, et al. (2007) ci21A/Asr1 expression influences glucose accumulation in potato tubers. Plant Mol Biol 63: 719-730.
    • (2007) Plant Mol Biol , vol.63 , pp. 719-730
    • Frankel, N.1    Nunes-Nesi, A.2    Balbo, I.3    Mazuch, J.4    Centeno, D.5
  • 7
    • 0141787935 scopus 로고    scopus 로고
    • A grape ASR protein involved in sugar and abscisic acid signaling
    • Cakir B, Agasse A, Gaillard C, Saumonneau A, Delrot S, et al. (2003) A grape ASR protein involved in sugar and abscisic acid signaling. Plant Cell 15: 2165-2180.
    • (2003) Plant Cell , vol.15 , pp. 2165-2180
    • Cakir, B.1    Agasse, A.2    Gaillard, C.3    Saumonneau, A.4    Delrot, S.5
  • 8
    • 0037248196 scopus 로고    scopus 로고
    • Sugar-regulated expression of a putative hexose transport gene in grape
    • Atanassova R, Leterrier M, Gaillard C, Agasse A, Sagot E, et al. (2003) Sugar-regulated expression of a putative hexose transport gene in grape. Plant Physiol 131: 326-334.
    • (2003) Plant Physiol , vol.131 , pp. 326-334
    • Atanassova, R.1    Leterrier, M.2    Gaillard, C.3    Agasse, A.4    Sagot, E.5
  • 9
    • 3242780721 scopus 로고    scopus 로고
    • The water- and salt-stress-regulated Asr1 (abscisic acid stress ripening) gene encodes a zinc-dependent DNA-binding protein
    • Kalifa Y, Gilad A, Konrad Z, Zaccai M, Scolnik PA, et al. (2004) The water- and salt-stress-regulated Asr1 (abscisic acid stress ripening) gene encodes a zinc-dependent DNA-binding protein. Biochem J 381: 373-378.
    • (2004) Biochem J , vol.381 , pp. 373-378
    • Kalifa, Y.1    Gilad, A.2    Konrad, Z.3    Zaccai, M.4    Scolnik, P.A.5
  • 10
    • 33745958973 scopus 로고    scopus 로고
    • Mapping the DNA- and zinc-binding domains of ASR1 (abscisic acid stress ripening), an abiotic-stress regulated plant specific protein
    • Rom S, Gilad A, Kalifa Y, Konrad Z, Karpasas MM, et al. (2006) Mapping the DNA- and zinc-binding domains of ASR1 (abscisic acid stress ripening), an abiotic-stress regulated plant specific protein. Biochimie 88: 621-628.
    • (2006) Biochimie , vol.88 , pp. 621-628
    • Rom, S.1    Gilad, A.2    Kalifa, Y.3    Konrad, Z.4    Karpasas, M.M.5
  • 11
    • 33845438869 scopus 로고    scopus 로고
    • Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss
    • Maskin L, Frankel N, Gudesblat G, Demergasso MJ, Pietrasanta LI, et al. (2007) Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss. Biochem Biophys Res Commun 352: 831-835.
    • (2007) Biochem Biophys Res Commun , vol.352 , pp. 831-835
    • Maskin, L.1    Frankel, N.2    Gudesblat, G.3    Demergasso, M.J.4    Pietrasanta, L.I.5
  • 12
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • Lesne S, Koh MT, Kotilinek L, Kayed R, Glabe CG, et al. (2006) A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440: 352-357.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3    Kayed, R.4    Glabe, C.G.5
  • 13
    • 79959423595 scopus 로고    scopus 로고
    • The structure of the nuclear pore complex
    • Hoelz A, Debler EW, Blobel G, (2011) The structure of the nuclear pore complex. Annu Rev Biochem 80: 613-643.
    • (2011) Annu Rev Biochem , vol.80 , pp. 613-643
    • Hoelz, A.1    Debler, E.W.2    Blobel, G.3
  • 14
    • 69849093363 scopus 로고    scopus 로고
    • Characterisation of the passive permeability barrier of nuclear pore complexes
    • Mohr D, Frey S, Fischer T, Guttler T, Gorlich D, (2009) Characterisation of the passive permeability barrier of nuclear pore complexes. EMBO J 28: 2541-2553.
    • (2009) EMBO J , vol.28 , pp. 2541-2553
    • Mohr, D.1    Frey, S.2    Fischer, T.3    Guttler, T.4    Gorlich, D.5
  • 15
    • 0039115156 scopus 로고    scopus 로고
    • Transport into and out of the cell nucleus
    • Gorlich D, (1998) Transport into and out of the cell nucleus. EMBO J 17: 2721-2727.
    • (1998) EMBO J , vol.17 , pp. 2721-2727
    • Gorlich, D.1
  • 16
    • 0031104648 scopus 로고    scopus 로고
    • Green-fluorescent protein fusions for efficient characterization of nuclear targeting
    • Grebenok RJ, Pierson E, Lambert GM, Gong F-C, Afonso CL, et al. (1997) Green-fluorescent protein fusions for efficient characterization of nuclear targeting. The Plant Journal 11: 573-586.
    • (1997) The Plant Journal , vol.11 , pp. 573-586
    • Grebenok, R.J.1    Pierson, E.2    Lambert, G.M.3    Gong, F.-C.4    Afonso, C.L.5
  • 17
    • 34250807710 scopus 로고    scopus 로고
    • The maximal size of protein to diffuse through the nuclear pore is larger than 60 kDa
    • Wang R, Brattain MG, (2007) The maximal size of protein to diffuse through the nuclear pore is larger than 60 kDa. FEBS Letters 581: 3164-3170.
    • (2007) FEBS Letters , vol.581 , pp. 3164-3170
    • Wang, R.1    Brattain, M.G.2
  • 18
    • 77956199192 scopus 로고    scopus 로고
    • Plant-mPLoc: a top-down strategy to augment the power for predicting plant protein subcellular localization
    • Chou KC, Shen HB, (2010) Plant-mPLoc: a top-down strategy to augment the power for predicting plant protein subcellular localization. PLoS One 5: e11335.
    • (2010) PLoS One , vol.5
    • Chou, K.C.1    Shen, H.B.2
  • 19
    • 77954274687 scopus 로고    scopus 로고
    • YLoc-an interpretable web server for predicting subcellular localization
    • Briesemeister S, Rahnenfuhrer J, Kohlbacher O, (2010) YLoc-an interpretable web server for predicting subcellular localization. Nucleic Acids Res 38: W497-502.
    • (2010) Nucleic Acids Res , vol.38
    • Briesemeister, S.1    Rahnenfuhrer, J.2    Kohlbacher, O.3
  • 20
    • 34248205175 scopus 로고    scopus 로고
    • Predicting nuclear localization
    • Hawkins J, Davis L, Boden M, (2007) Predicting nuclear localization. J Proteome Res 6: 1402-1409.
    • (2007) J Proteome Res , vol.6 , pp. 1402-1409
    • Hawkins, J.1    Davis, L.2    Boden, M.3
  • 21
    • 77949498332 scopus 로고    scopus 로고
    • Expanding the Definition of the Classical Bipartite Nuclear Localization Signal
    • Lange A, McLane LM, Mills RE, Devine SE, Corbett AH, (2010) Expanding the Definition of the Classical Bipartite Nuclear Localization Signal. Traffic 11: 311-323.
    • (2010) Traffic , vol.11 , pp. 311-323
    • Lange, A.1    McLane, L.M.2    Mills, R.E.3    Devine, S.E.4    Corbett, A.H.5
  • 22
    • 0028500170 scopus 로고
    • The small, versatile pPZP family of Agrobacterium binary vectors for plant transformation
    • Hajdukiewicz P, Svab Z, Maliga P, (1994) The small, versatile pPZP family of Agrobacterium binary vectors for plant transformation. Plant Mol Biol 25: 989-994.
    • (1994) Plant Mol Biol , vol.25 , pp. 989-994
    • Hajdukiewicz, P.1    Svab, Z.2    Maliga, P.3
  • 23
    • 34547677722 scopus 로고    scopus 로고
    • Development of series of gateway binary vectors, pGWBs, for realizing efficient construction of fusion genes for plant transformation
    • Nakagawa T, Kurose T, Hino T, Tanaka K, Kawamukai M, et al. (2007) Development of series of gateway binary vectors, pGWBs, for realizing efficient construction of fusion genes for plant transformation. J Biosci Bioeng 104: 34-41.
    • (2007) J Biosci Bioeng , vol.104 , pp. 34-41
    • Nakagawa, T.1    Kurose, T.2    Hino, T.3    Tanaka, K.4    Kawamukai, M.5
  • 24
    • 0028805527 scopus 로고
    • Moderate-temperature polymerization of LR White in a nitrogen atmosphere
    • Harris KF, Pesic-Van Esbroeck Z, Duffus JE, (1995) Moderate-temperature polymerization of LR White in a nitrogen atmosphere. Microsc Res Tech 32: 264-265.
    • (1995) Microsc Res Tech , vol.32 , pp. 264-265
    • Harris, K.F.1    Pesic-Van Esbroeck, Z.2    Duffus, J.E.3
  • 25
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte S, Cordelières FP, (2006) A guided tour into subcellular colocalization analysis in light microscopy. Journal of Microscopy 224: 213-232.
    • (2006) Journal of Microscopy , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelières, F.P.2
  • 26
    • 77950668357 scopus 로고    scopus 로고
    • Protocol: fine-tuning of a Chromatin Immunoprecipitation (ChIP) protocol in tomato
    • Ricardi M, Gonzalez R, Iusem N, (2010) Protocol: fine-tuning of a Chromatin Immunoprecipitation (ChIP) protocol in tomato. Plant Methods 6: 11.
    • (2010) Plant Methods , vol.6 , pp. 11
    • Ricardi, M.1    Gonzalez, R.2    Iusem, N.3
  • 27
    • 15544390874 scopus 로고    scopus 로고
    • A lily pollen ASR protein localizes to both cytoplasm and nuclei requiring a nuclear localization signal
    • Wang H-J, Hsu C-M, Jauh GY, Wang C-S, (2005) A lily pollen ASR protein localizes to both cytoplasm and nuclei requiring a nuclear localization signal. Physiologia Plantarum 123: 314-320.
    • (2005) Physiologia Plantarum , vol.123 , pp. 314-320
    • Wang, H.-J.1    Hsu, C.-M.2    Jauh, G.Y.3    Wang, C.-S.4
  • 28
    • 70349601671 scopus 로고    scopus 로고
    • New GATEWAY vectors for high throughput analyses of protein-protein interactions by bimolecular fluorescence complementation
    • Gehl C, Waadt R, Kudla J, Mendel RR, Hansch R, (2009) New GATEWAY vectors for high throughput analyses of protein-protein interactions by bimolecular fluorescence complementation. Mol Plant 2: 1051-1058.
    • (2009) Mol Plant , vol.2 , pp. 1051-1058
    • Gehl, C.1    Waadt, R.2    Kudla, J.3    Mendel, R.R.4    Hansch, R.5
  • 29
    • 33745785300 scopus 로고    scopus 로고
    • Visualization of molecular interactions by fluorescence complementation
    • Kerppola TK, (2006) Visualization of molecular interactions by fluorescence complementation. Nat Rev Mol Cell Biol 7: 449-456.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 449-456
    • Kerppola, T.K.1
  • 30
    • 85056048375 scopus 로고    scopus 로고
    • Predominantly Cytoplasmic Localization in Yeast of ASR1, a Non-Receptor Transcription Factor from Plants
    • Urtasun N, Correa Garcia S, Iusem ND, Bermudez Moretti M, (2010) Predominantly Cytoplasmic Localization in Yeast of ASR1, a Non-Receptor Transcription Factor from Plants. Open Biochem J 4: 68-71.
    • (2010) Open Biochem J , vol.4 , pp. 68-71
    • Urtasun, N.1    Correa Garcia, S.2    Iusem, N.D.3    Bermudez Moretti, M.4
  • 31
    • 0042977521 scopus 로고    scopus 로고
    • The ins and outs of STAT1 nuclear transport
    • McBride KM, Reich NC, (2003) The ins and outs of STAT1 nuclear transport. Sci STKE 2003: RE13.
    • (2003) Sci STKE , vol.2003
    • McBride, K.M.1    Reich, N.C.2
  • 32
    • 79952777363 scopus 로고    scopus 로고
    • The role of the N-terminal domain in dimerization and nucleocytoplasmic shuttling of latent STAT3
    • Vogt M, Domoszlai T, Kleshchanok D, Lehmann S, Schmitt A, et al. (2011) The role of the N-terminal domain in dimerization and nucleocytoplasmic shuttling of latent STAT3. J Cell Sci 124: 900-909.
    • (2011) J Cell Sci , vol.124 , pp. 900-909
    • Vogt, M.1    Domoszlai, T.2    Kleshchanok, D.3    Lehmann, S.4    Schmitt, A.5
  • 33
    • 77449122749 scopus 로고    scopus 로고
    • ERK Nuclear Translocation Is Dimerization-independent but Controlled by the Rate of Phosphorylation
    • Lidke DS, Huang F, Post JN, Rieger B, Wilsbacher J, et al. (2010) ERK Nuclear Translocation Is Dimerization-independent but Controlled by the Rate of Phosphorylation. Journal of Biological Chemistry 285: 3092-3102.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 3092-3102
    • Lidke, D.S.1    Huang, F.2    Post, J.N.3    Rieger, B.4    Wilsbacher, J.5


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