메뉴 건너뛰기




Volumn 13, Issue 1, 2013, Pages

Recovery from heat, salt and osmotic stress in Physcomitrella patens requires a functional small heat shock protein PpHsp16.4

Author keywords

Osmotic stress; Physcomitrella patens; Salinity; Small heat shock proteins

Indexed keywords

BRYOPHYTA; EMBRYOPHYTA; PHYSCOMITRELLA PATENS;

EID: 84887039571     PISSN: None     EISSN: 14712229     Source Type: Journal    
DOI: 10.1186/1471-2229-13-174     Document Type: Article
Times cited : (53)

References (79)
  • 1
    • 1642441342 scopus 로고    scopus 로고
    • Molecular genetic perspectives on cross-talk and specificity in abiotic stress signalling in plants
    • Chinnusamy V, Schumaker K, Zhu JK. Molecular genetic perspectives on cross-talk and specificity in abiotic stress signalling in plants. J Exp Bot 2004, 55:225-236.
    • (2004) J Exp Bot , vol.55 , pp. 225-236
    • Chinnusamy, V.1    Schumaker, K.2    Zhu, J.K.3
  • 2
    • 30744466639 scopus 로고    scopus 로고
    • Desiccation tolerance in bryophytes: a reflection of the primitive strategy for plant survival in dehydrating habitats?
    • 10.1093/icb/45.5.788, 21676830
    • Oliver MJ, Velten J, Mishler BD. Desiccation tolerance in bryophytes: a reflection of the primitive strategy for plant survival in dehydrating habitats?. Integr Comp Biol 2005, 45:788-799. 10.1093/icb/45.5.788, 21676830.
    • (2005) Integr Comp Biol , vol.45 , pp. 788-799
    • Oliver, M.J.1    Velten, J.2    Mishler, B.D.3
  • 3
    • 0034028259 scopus 로고    scopus 로고
    • Molecular responses to dehydration and low temperature: differences and cross-talk between two stress signaling pathways
    • Shinozaki K, Yamaguchi-Shinozaki K. Molecular responses to dehydration and low temperature: differences and cross-talk between two stress signaling pathways. Curr Opin Plant Biol 2000, 3:217-223.
    • (2000) Curr Opin Plant Biol , vol.3 , pp. 217-223
    • Shinozaki, K.1    Yamaguchi-Shinozaki, K.2
  • 4
    • 0031081346 scopus 로고    scopus 로고
    • Plant responses to water deficit
    • Bray EA. Plant responses to water deficit. Trends Plant Sci 1997, 2:48-54.
    • (1997) Trends Plant Sci , vol.2 , pp. 48-54
    • Bray, E.A.1
  • 5
    • 0036999615 scopus 로고    scopus 로고
    • Salt and drought stress signal transduction in plants
    • 10.1146/annurev.arplant.53.091401.143329, 3128348, 12221975
    • Zhu JK. Salt and drought stress signal transduction in plants. Annu Rev Plant Biol 2002, 53:247-273. 10.1146/annurev.arplant.53.091401.143329, 3128348, 12221975.
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 247-273
    • Zhu, J.K.1
  • 7
    • 84857964166 scopus 로고    scopus 로고
    • Drought, salt, and temperature stress-induced metabolic rearrangements and regulatory networks
    • 10.1093/jxb/err460, 22291134
    • Krasensky J, Jonak C. Drought, salt, and temperature stress-induced metabolic rearrangements and regulatory networks. J Exp Bot 2012, 63:1593-1608. 10.1093/jxb/err460, 22291134.
    • (2012) J Exp Bot , vol.63 , pp. 1593-1608
    • Krasensky, J.1    Jonak, C.2
  • 8
    • 0034815248 scopus 로고    scopus 로고
    • The expanding family of Arabidopsis thaliana small heat stress proteins and a new family of proteins containing alpha-crystallin domains (Acd proteins)
    • Scharf KD, Siddique M, Vierling E. The expanding family of Arabidopsis thaliana small heat stress proteins and a new family of proteins containing alpha-crystallin domains (Acd proteins). Cell Stress Chaperon 2001, 6:225-237.
    • (2001) Cell Stress Chaperon , vol.6 , pp. 225-237
    • Scharf, K.D.1    Siddique, M.2    Vierling, E.3
  • 9
    • 0031432208 scopus 로고    scopus 로고
    • Stable transformation of an Arabidopsis cell suspension culture with firefly luciferase providing a cellular system for analysis of chaperone activity in vivo
    • 157066, 9437862
    • Forreiter C, Kirschner M, Nover L. Stable transformation of an Arabidopsis cell suspension culture with firefly luciferase providing a cellular system for analysis of chaperone activity in vivo. Plant Cell 1997, 9:2171-2181. 157066, 9437862.
    • (1997) Plant Cell , vol.9 , pp. 2171-2181
    • Forreiter, C.1    Kirschner, M.2    Nover, L.3
  • 10
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • 10.1093/emboj/16.3.659, 1169668, 9034347
    • Lee GJ, Roseman AM, Saibil HR, Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J 1997, 16:659-671. 10.1093/emboj/16.3.659, 1169668, 9034347.
    • (1997) EMBO J , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 11
    • 0031757704 scopus 로고    scopus 로고
    • The small, methionine-rich chloroplast heat-shock protein protects photosystem II electron transport during heat stress
    • 10.1104/pp.116.1.439, 35186, 9449851
    • Heckathorn SA, Downs CA, Sharkey TD, Coleman JS. The small, methionine-rich chloroplast heat-shock protein protects photosystem II electron transport during heat stress. Plant Physiol 1998, 116:439-444. 10.1104/pp.116.1.439, 35186, 9449851.
    • (1998) Plant Physiol , vol.116 , pp. 439-444
    • Heckathorn, S.A.1    Downs, C.A.2    Sharkey, T.D.3    Coleman, J.S.4
  • 12
    • 0033794820 scopus 로고    scopus 로고
    • Cytosolic heat-stress proteins Hsp17.7 class I and Hsp17.3 class II of tomato act as molecular chaperones in vivo
    • 10.1007/s004250000315, 11030557
    • Löw D, Brandle K, Nover L, Forreiter C. Cytosolic heat-stress proteins Hsp17.7 class I and Hsp17.3 class II of tomato act as molecular chaperones in vivo. Planta 2000, 211:575-582. 10.1007/s004250000315, 11030557.
    • (2000) Planta , vol.211 , pp. 575-582
    • Löw, D.1    Brandle, K.2    Nover, L.3    Forreiter, C.4
  • 13
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the alpha-crystallin-small heat-shock protein superfamily
    • 10.1016/S0141-8130(98)00013-0, 9650070
    • de Jong WW, Caspers GJ, Leunissen JA. Genealogy of the alpha-crystallin-small heat-shock protein superfamily. Int J Biol Macromol 1998, 22:151-162. 10.1016/S0141-8130(98)00013-0, 9650070.
    • (1998) Int J Biol Macromol , vol.22 , pp. 151-162
    • de Jong, W.W.1    Caspers, G.J.2    Leunissen, J.A.3
  • 14
    • 84861619255 scopus 로고    scopus 로고
    • Evolution and functional diversification of the small heat shock protein/α-crystallin family in higher plants
    • 10.1007/s00425-011-1575-9, 22210597
    • Bondino HG, Valle EM, Ten Have A. Evolution and functional diversification of the small heat shock protein/α-crystallin family in higher plants. Planta 2012, 235:1299-1313. 10.1007/s00425-011-1575-9, 22210597.
    • (2012) Planta , vol.235 , pp. 1299-1313
    • Bondino, H.G.1    Valle, E.M.2    Ten Have, A.3
  • 15
    • 84872308465 scopus 로고    scopus 로고
    • The evolution, function, structure, and expression of the plant sHSPs
    • 10.1093/jxb/ers355, 23255280
    • Waters ER. The evolution, function, structure, and expression of the plant sHSPs. J Exp Bot 2013, 64:391-403. 10.1093/jxb/ers355, 23255280.
    • (2013) J Exp Bot , vol.64 , pp. 391-403
    • Waters, E.R.1
  • 16
    • 0032090396 scopus 로고    scopus 로고
    • Expression of small heat-shock proteins at low temperatures. A possible role in protecting against chilling injuries
    • 10.1104/pp.117.2.651, 34985, 9625718
    • Sabehat A, Lurie S, Weiss D. Expression of small heat-shock proteins at low temperatures. A possible role in protecting against chilling injuries. Plant Physiol 1998, 117:651-658. 10.1104/pp.117.2.651, 34985, 9625718.
    • (1998) Plant Physiol , vol.117 , pp. 651-658
    • Sabehat, A.1    Lurie, S.2    Weiss, D.3
  • 17
    • 0002844238 scopus 로고
    • Production and action of active oxygen species in photosynthetic tissues
    • Florida: CRC Press, Foyer CH, Mullineaux PM
    • Asada K. Production and action of active oxygen species in photosynthetic tissues. Causes of photooxidative stress and amelioration of defense systems in plants 1994, 77-104. Florida: CRC Press, Foyer CH, Mullineaux PM.
    • (1994) Causes of photooxidative stress and amelioration of defense systems in plants , pp. 77-104
    • Asada, K.1
  • 18
    • 0027131328 scopus 로고
    • Tissue-specific expression of sunflower heat shock proteins in response to water stress
    • Almoguera C, Coca MA, Jordano J. Tissue-specific expression of sunflower heat shock proteins in response to water stress. Plant J 1993, 4:947-958.
    • (1993) Plant J , vol.4 , pp. 947-958
    • Almoguera, C.1    Coca, M.A.2    Jordano, J.3
  • 19
    • 0029616226 scopus 로고
    • Constitutive expression of small heat shock proteins in vegetative tissues of the resurrection plant Craterostigma plantagineum
    • 10.1007/BF00014981, 8555452
    • Alamillo J, Almoguera C, Bartels D, Jordano J. Constitutive expression of small heat shock proteins in vegetative tissues of the resurrection plant Craterostigma plantagineum. Plant Mol Biol 1995, 29:1093-1099. 10.1007/BF00014981, 8555452.
    • (1995) Plant Mol Biol , vol.29 , pp. 1093-1099
    • Alamillo, J.1    Almoguera, C.2    Bartels, D.3    Jordano, J.4
  • 20
    • 0344172562 scopus 로고    scopus 로고
    • The chloroplast small heat shock protein undergoes oxidation-dependent conformational changes and may protect plants from oxidative stress
    • Harndahl U, Hall RB, Osteryoung KW, Vierling E, Bornman JF, Sundby C. The chloroplast small heat shock protein undergoes oxidation-dependent conformational changes and may protect plants from oxidative stress. Cell Stress Chaperon 1999, 4:129-138.
    • (1999) Cell Stress Chaperon , vol.4 , pp. 129-138
    • Harndahl, U.1    Hall, R.B.2    Osteryoung, K.W.3    Vierling, E.4    Bornman, J.F.5    Sundby, C.6
  • 21
    • 0034958914 scopus 로고    scopus 로고
    • Mitochondrial adaptations to NaCl. Complex I is protected by anti-oxidants and small heat shock proteins, whereas complex II is protected by proline and betaine
    • 10.1104/pp.126.3.1266, 116483, 11457977
    • Hamilton EW, Heckathorn SA. Mitochondrial adaptations to NaCl. Complex I is protected by anti-oxidants and small heat shock proteins, whereas complex II is protected by proline and betaine. Plant Physiol 2001, 126:1266-1274. 10.1104/pp.126.3.1266, 116483, 11457977.
    • (2001) Plant Physiol , vol.126 , pp. 1266-1274
    • Hamilton, E.W.1    Heckathorn, S.A.2
  • 22
    • 0037136230 scopus 로고    scopus 로고
    • Small heat shock proteins and stress tolerance in plants
    • 10.1016/S0167-4781(02)00417-7, 12151089
    • Sun W, Van Montagu M, Verbruggen N. Small heat shock proteins and stress tolerance in plants. Biochim Biophys Acta 2002, 1577:1-9. 10.1016/S0167-4781(02)00417-7, 12151089.
    • (2002) Biochim Biophys Acta , vol.1577 , pp. 1-9
    • Sun, W.1    Van Montagu, M.2    Verbruggen, N.3
  • 23
    • 0034004638 scopus 로고    scopus 로고
    • The expression of small heat shock proteins in seeds responds to discrete developmental signals and suggests a general protective role in desiccation tolerance
    • 10.1104/pp.122.4.1099, 58944, 10759505
    • Wehmeyer N, Vierling E. The expression of small heat shock proteins in seeds responds to discrete developmental signals and suggests a general protective role in desiccation tolerance. Plant Physiol 2000, 122:1099-1108. 10.1104/pp.122.4.1099, 58944, 10759505.
    • (2000) Plant Physiol , vol.122 , pp. 1099-1108
    • Wehmeyer, N.1    Vierling, E.2
  • 24
    • 0029564954 scopus 로고
    • Heat shock transcription factors: structure and regulation
    • Wu C. Heat shock transcription factors: structure and regulation. Annu Rev Cell Develop Biol 1995, 11:441-469.
    • (1995) Annu Rev Cell Develop Biol , vol.11 , pp. 441-469
    • Wu, C.1
  • 25
    • 0032133306 scopus 로고    scopus 로고
    • Regulation of the heat-shock response
    • 10.1104/pp.117.4.1135, 1539185, 9701569
    • Schöffl F, Prändl R, Reindl A. Regulation of the heat-shock response. Plant Physiol 1998, 117:1135-1141. 10.1104/pp.117.4.1135, 1539185, 9701569.
    • (1998) Plant Physiol , vol.117 , pp. 1135-1141
    • Schöffl, F.1    Prändl, R.2    Reindl, A.3
  • 26
    • 0020184673 scopus 로고
    • A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene
    • 10.1016/0092-8674(82)90249-5, 6814763
    • Pelham HR. A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene. Cell 1982, 30:517-528. 10.1016/0092-8674(82)90249-5, 6814763.
    • (1982) Cell , vol.30 , pp. 517-528
    • Pelham, H.R.1
  • 27
    • 34648830573 scopus 로고    scopus 로고
    • The diversity of plant heat stress transcription factors
    • 10.1016/j.tplants.2007.08.014, 17826296
    • von Koskull-Doring P, Scharf K-D, Nover L. The diversity of plant heat stress transcription factors. Trends Plant Sci 2007, 12:452-457. 10.1016/j.tplants.2007.08.014, 17826296.
    • (2007) Trends Plant Sci , vol.12 , pp. 452-457
    • von Koskull-Doring, P.1    Scharf, K.-D.2    Nover, L.3
  • 28
    • 34248207000 scopus 로고    scopus 로고
    • A novel transcriptional cascade regulating expression of heat stress proteins during seed development of Arabidopsis
    • 10.1105/tpc.106.048165, 1820961, 17220197
    • Kotak S, Vierling E, Bäumlein H, Koskull-Döring PV. A novel transcriptional cascade regulating expression of heat stress proteins during seed development of Arabidopsis. Plant Cell 2007, 19:182-195. 10.1105/tpc.106.048165, 1820961, 17220197.
    • (2007) Plant Cell , vol.19 , pp. 182-195
    • Kotak, S.1    Vierling, E.2    Bäumlein, H.3    Koskull-Döring, P.V.4
  • 29
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • 10.1093/emboj/16.2.221, 1169629, 9029143
    • Ehrnsperger M, Graber S, Gaestel M, Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J 1997, 16:221-229. 10.1093/emboj/16.2.221, 1169629, 9029143.
    • (1997) EMBO J , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 30
    • 0032079487 scopus 로고    scopus 로고
    • The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • 10.1074/jbc.273.18.11032, 9556585
    • Veinger L, Diamant S, Buchner J, Goloubinoff P. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J Biol Chem 1998, 273:11032-11037. 10.1074/jbc.273.18.11032, 9556585.
    • (1998) J Biol Chem , vol.273 , pp. 11032-11037
    • Veinger, L.1    Diamant, S.2    Buchner, J.3    Goloubinoff, P.4
  • 31
    • 0033765314 scopus 로고    scopus 로고
    • A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein
    • 10.1104/pp.122.1.189, 58857, 10631262
    • Lee GJ, Vierling E. A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein. Plant Physiol 2000, 122:189-198. 10.1104/pp.122.1.189, 58857, 10631262.
    • (2000) Plant Physiol , vol.122 , pp. 189-198
    • Lee, G.J.1    Vierling, E.2
  • 32
    • 0034681446 scopus 로고    scopus 로고
    • Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins
    • 10.1074/jbc.275.7.4565, 10671481
    • Reddy GB, Das KP, Petrash JM, Surewicz WK. Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins. J Biol Chem 2000, 275:4565-4570. 10.1074/jbc.275.7.4565, 10671481.
    • (2000) J Biol Chem , vol.275 , pp. 4565-4570
    • Reddy, G.B.1    Das, K.P.2    Petrash, J.M.3    Surewicz, W.K.4
  • 33
    • 33846945050 scopus 로고    scopus 로고
    • The small heat shock proteins and their clients
    • 10.1007/s00018-006-6321-2, 17187175
    • Nakamoto H, Vigh L. The small heat shock proteins and their clients. Cell Mol Life Sci 2007, 64:294-306. 10.1007/s00018-006-6321-2, 17187175.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 294-306
    • Nakamoto, H.1    Vigh, L.2
  • 34
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters ER, Lee GJ, Vierling E. Evolution, structure and function of the small heat shock proteins in plants. J Exp Bot 1996, 47:325-338.
    • (1996) J Exp Bot , vol.47 , pp. 325-338
    • Waters, E.R.1    Lee, G.J.2    Vierling, E.3
  • 35
    • 0042733148 scopus 로고    scopus 로고
    • Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
    • Mogk A, Schlieker C, Friedrich KL, Schonfeld HJ, Vierling E, Bukau B. Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J Bioll Chem 2003, 278:31033-31042.
    • (2003) J Bioll Chem , vol.278 , pp. 31033-31042
    • Mogk, A.1    Schlieker, C.2    Friedrich, K.L.3    Schonfeld, H.J.4    Vierling, E.5    Bukau, B.6
  • 36
    • 0031170922 scopus 로고    scopus 로고
    • Efficient gene targeting in the moss Physcomitrella patens
    • 10.1046/j.1365-313X.1997.11061195.x, 9225463
    • Schaefer DG, Zryd JP. Efficient gene targeting in the moss Physcomitrella patens. Plant J 1997, 11:1195-1206. 10.1046/j.1365-313X.1997.11061195.x, 9225463.
    • (1997) Plant J , vol.11 , pp. 1195-1206
    • Schaefer, D.G.1    Zryd, J.P.2
  • 37
    • 33644913648 scopus 로고    scopus 로고
    • A dehydrin gene in Physcomitrella patens is required for salt and osmotic stress tolerance
    • 10.1111/j.1365-313X.2005.02603.x, 16367967
    • Saavedra L, Svensson J, Carballo V, Izmendi D, Welin B, Vidal S. A dehydrin gene in Physcomitrella patens is required for salt and osmotic stress tolerance. Plant J 2006, 45:237-249. 10.1111/j.1365-313X.2005.02603.x, 16367967.
    • (2006) Plant J , vol.45 , pp. 237-249
    • Saavedra, L.1    Svensson, J.2    Carballo, V.3    Izmendi, D.4    Welin, B.5    Vidal, S.6
  • 38
    • 77951628472 scopus 로고    scopus 로고
    • Between a rock and a dry place: the water-stressed moss
    • 10.1093/mp/ssp018, 19825631
    • Charron AJ, Quatrano RS. Between a rock and a dry place: the water-stressed moss. Mol Plant 2009, 2:478-486. 10.1093/mp/ssp018, 19825631.
    • (2009) Mol Plant , vol.2 , pp. 478-486
    • Charron, A.J.1    Quatrano, R.S.2
  • 39
    • 14944380630 scopus 로고    scopus 로고
    • Physcomitrella patens is highly tolerant against drought, salt and osmotic stress
    • 10.1007/s00425-004-1351-1, 15322883
    • Frank W, Ratnadewi D, Reski R. Physcomitrella patens is highly tolerant against drought, salt and osmotic stress. Planta 2005, 220:384-394. 10.1007/s00425-004-1351-1, 15322883.
    • (2005) Planta , vol.220 , pp. 384-394
    • Frank, W.1    Ratnadewi, D.2    Reski, R.3
  • 40
    • 65249148430 scopus 로고    scopus 로고
    • Exploring the mechanism of Physcomitrella patens desiccation tolerance through a proteomic strategy
    • 10.1104/pp.108.131714, 2663739, 19211702
    • Wang XQ, Yang PF, Liu Z, Liu WZ, Hu Y, Chen H, Kuang TY, Pei ZM, Shen SH, He YK. Exploring the mechanism of Physcomitrella patens desiccation tolerance through a proteomic strategy. Plant Physiol 2009, 149:1739-1750. 10.1104/pp.108.131714, 2663739, 19211702.
    • (2009) Plant Physiol , vol.149 , pp. 1739-1750
    • Wang, X.Q.1    Yang, P.F.2    Liu, Z.3    Liu, W.Z.4    Hu, Y.5    Chen, H.6    Kuang, T.Y.7    Pei, Z.M.8    Shen, S.H.9    He, Y.K.10
  • 42
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • 10.1093/nar/25.24.4876, 147148, 9396791
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997, 25:4876-4882. 10.1093/nar/25.24.4876, 147148, 9396791.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 43
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • 10.1093/molbev/msr121, 3203626, 21546353
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 2011, 28:2731-2739. 10.1093/molbev/msr121, 3203626, 21546353.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 44
    • 64749094910 scopus 로고    scopus 로고
    • Genevestigator transcriptome meta-analysis and biomarker search using rice and barley gene expression databases
    • 10.1093/mp/ssn048, 19825587
    • Zimmermann P, Laule O, Schmitz J, Hruz T, Bleuler S, Gruissem W. Genevestigator transcriptome meta-analysis and biomarker search using rice and barley gene expression databases. Mol Plant 2008, 1:851-857. 10.1093/mp/ssn048, 19825587.
    • (2008) Mol Plant , vol.1 , pp. 851-857
    • Zimmermann, P.1    Laule, O.2    Schmitz, J.3    Hruz, T.4    Bleuler, S.5    Gruissem, W.6
  • 45
  • 47
    • 0034710922 scopus 로고    scopus 로고
    • Molecular spectroscopy and dynamics of intrinsically fluorescent proteins: coral red (dsRed) and yellow (Citrine)
    • 10.1073/pnas.97.22.11996, 17283, 11050231
    • Heikal AA, Hess ST, Baird GS, Tsien RY, Webb WW. Molecular spectroscopy and dynamics of intrinsically fluorescent proteins: coral red (dsRed) and yellow (Citrine). Proc Natl Acad Sci USA 2000, 97:11996-12001. 10.1073/pnas.97.22.11996, 17283, 11050231.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11996-12001
    • Heikal, A.A.1    Hess, S.T.2    Baird, G.S.3    Tsien, R.Y.4    Webb, W.W.5
  • 48
    • 33845653228 scopus 로고    scopus 로고
    • The mechanism of gene targeting in Physcomitrella patens: homologous recombination, concatenation and multiple integration
    • 10.1093/nar/gkl832, 1693892, 17090599
    • Kamisugi Y, Schlink K, Rensing SA, Schween G, von Stackelberg M, Cuming AC, Reski R, Cove DJ. The mechanism of gene targeting in Physcomitrella patens: homologous recombination, concatenation and multiple integration. Nucleic Acids Res 2006, 34:6205-6214. 10.1093/nar/gkl832, 1693892, 17090599.
    • (2006) Nucleic Acids Res , vol.34 , pp. 6205-6214
    • Kamisugi, Y.1    Schlink, K.2    Rensing, S.A.3    Schween, G.4    von Stackelberg, M.5    Cuming, A.C.6    Reski, R.7    Cove, D.J.8
  • 49
    • 51649117559 scopus 로고    scopus 로고
    • Proteomics applied on plant abiotic stresses: role of heat shock proteins (HSP)
    • 10.1016/j.jprot.2008.07.005, 18718564
    • Timperio AM, Egidi MG, Zolla L. Proteomics applied on plant abiotic stresses: role of heat shock proteins (HSP). J proteomics 2008, 71:391-411. 10.1016/j.jprot.2008.07.005, 18718564.
    • (2008) J proteomics , vol.71 , pp. 391-411
    • Timperio, A.M.1    Egidi, M.G.2    Zolla, L.3
  • 50
    • 34347265817 scopus 로고    scopus 로고
    • Transcriptional profiling of Arabidopsis heat shock proteins and transcription factors reveals extensive overlap between heat and non-heat stress response pathways
    • 10.1186/1471-2164-8-125, 1887538, 17519032
    • Swindell W, Huebner M, Weber A. Transcriptional profiling of Arabidopsis heat shock proteins and transcription factors reveals extensive overlap between heat and non-heat stress response pathways. BMC Genomics 2007, 8:125. 10.1186/1471-2164-8-125, 1887538, 17519032.
    • (2007) BMC Genomics , vol.8 , pp. 125
    • Swindell, W.1    Huebner, M.2    Weber, A.3
  • 52
    • 67349254489 scopus 로고    scopus 로고
    • Comparative analysis of the small heat shock proteins in three angiosperm genomes identifies new subfamilies and reveals diverse evolutionary patterns
    • Waters E, Aevermann B, Sanders-Reed Z. Comparative analysis of the small heat shock proteins in three angiosperm genomes identifies new subfamilies and reveals diverse evolutionary patterns. Cell Stress Chaperon 2008, 13:127-142.
    • (2008) Cell Stress Chaperon , vol.13 , pp. 127-142
    • Waters, E.1    Aevermann, B.2    Sanders-Reed, Z.3
  • 53
    • 43049145797 scopus 로고    scopus 로고
    • Generation of superoxide anion in chloroplasts of Arabidopsis thaliana during active photosynthesis: a focus on rapidly induced genes
    • 10.1007/s11103-007-9274-4, 2758387, 18158584
    • Scarpeci TE, Zanor MI, Carrillo N, Mueller-Roeber B, Valle EM. Generation of superoxide anion in chloroplasts of Arabidopsis thaliana during active photosynthesis: a focus on rapidly induced genes. Plant Mol Biol 2008, 66:361-378. 10.1007/s11103-007-9274-4, 2758387, 18158584.
    • (2008) Plant Mol Biol , vol.66 , pp. 361-378
    • Scarpeci, T.E.1    Zanor, M.I.2    Carrillo, N.3    Mueller-Roeber, B.4    Valle, E.M.5
  • 54
    • 4644304481 scopus 로고    scopus 로고
    • Reactive oxygen gene network of plants
    • 10.1016/j.tplants.2004.08.009, 15465684
    • Mittler R, Vanderauwera S, Gollery M, Van Breusegem F. Reactive oxygen gene network of plants. Trends Plant Sci 2004, 9:490-498. 10.1016/j.tplants.2004.08.009, 15465684.
    • (2004) Trends Plant Sci , vol.9 , pp. 490-498
    • Mittler, R.1    Vanderauwera, S.2    Gollery, M.3    Van Breusegem, F.4
  • 55
    • 33748143367 scopus 로고    scopus 로고
    • Could heat shock transcription factors function as hydrogen peroxide sensors in plants?
    • 10.1093/aob/mcl107, 2803459, 16740587
    • Miller G, Mittler R. Could heat shock transcription factors function as hydrogen peroxide sensors in plants?. Ann Bot 2006, 98:279-288. 10.1093/aob/mcl107, 2803459, 16740587.
    • (2006) Ann Bot , vol.98 , pp. 279-288
    • Miller, G.1    Mittler, R.2
  • 56
    • 32944457560 scopus 로고    scopus 로고
    • Dual role for tomato heat shock protein 21: protecting photosystem II from oxidative stress and promoting color changes during fruit maturation
    • 10.1105/tpc.105.031914, 1143080, 15879560
    • Neta-Sharir I, Isaacson T, Lurie S, Weiss D. Dual role for tomato heat shock protein 21: protecting photosystem II from oxidative stress and promoting color changes during fruit maturation. Plant Cell 2005, 17:1829-1838. 10.1105/tpc.105.031914, 1143080, 15879560.
    • (2005) Plant Cell , vol.17 , pp. 1829-1838
    • Neta-Sharir, I.1    Isaacson, T.2    Lurie, S.3    Weiss, D.4
  • 57
    • 0032005909 scopus 로고    scopus 로고
    • Accumulation of small heat shock proteins, including mitochondrial HSP22, induced by oxidative stress and adaptive response in tomato cells
    • 10.1046/j.1365-313X.1998.00056.x, 9680997
    • Banzet N, Richaud C, Deveaux Y, Kazmaier M, Gagnon J, Triantaphylides C. Accumulation of small heat shock proteins, including mitochondrial HSP22, induced by oxidative stress and adaptive response in tomato cells. Plant J 1998, 13:519-527. 10.1046/j.1365-313X.1998.00056.x, 9680997.
    • (1998) Plant J , vol.13 , pp. 519-527
    • Banzet, N.1    Richaud, C.2    Deveaux, Y.3    Kazmaier, M.4    Gagnon, J.5    Triantaphylides, C.6
  • 58
    • 2342510197 scopus 로고    scopus 로고
    • Thermotolerance and antioxidant systems in Agrostis stolonifera: involvement of salicylic acid, abscisic acid, calcium, hydrogen peroxide, and ethylene
    • 10.1078/0176-1617-01239, 15128028
    • Larkindale J, Huang B. Thermotolerance and antioxidant systems in Agrostis stolonifera: involvement of salicylic acid, abscisic acid, calcium, hydrogen peroxide, and ethylene. J Plant Physiol 2004, 161:405-413. 10.1078/0176-1617-01239, 15128028.
    • (2004) J Plant Physiol , vol.161 , pp. 405-413
    • Larkindale, J.1    Huang, B.2
  • 59
    • 26944443125 scopus 로고    scopus 로고
    • Heat stress phenotypes of Arabidopsis mutants implicate multiple signaling pathways in the acquisition of thermotolerance
    • 10.1104/pp.105.062257, 1150405, 15923322
    • Larkindale J, Hall JD, Knight MR, Vierling E. Heat stress phenotypes of Arabidopsis mutants implicate multiple signaling pathways in the acquisition of thermotolerance. Plant Physiol 2005, 138:882-897. 10.1104/pp.105.062257, 1150405, 15923322.
    • (2005) Plant Physiol , vol.138 , pp. 882-897
    • Larkindale, J.1    Hall, J.D.2    Knight, M.R.3    Vierling, E.4
  • 60
    • 2342612864 scopus 로고    scopus 로고
    • Salicylic acid dependent signaling promotes basal thermotolerance but is not essential for acquired thermotolerance in Arabidopsis thaliana
    • 10.1111/j.1365-313X.2004.02054.x, 15086804
    • Clarke SM, Mur LAJ, Wood JE, Scott IM. Salicylic acid dependent signaling promotes basal thermotolerance but is not essential for acquired thermotolerance in Arabidopsis thaliana. Plant J 2004, 38:432-447. 10.1111/j.1365-313X.2004.02054.x, 15086804.
    • (2004) Plant J , vol.38 , pp. 432-447
    • Clarke, S.M.1    Mur, L.A.J.2    Wood, J.E.3    Scott, I.M.4
  • 61
    • 33750689502 scopus 로고    scopus 로고
    • Induction of a cDNA clone from rice encoding a class II small heat shock protein by heat stress, mechanical injury, and salicylic acid
    • Chang P-FL JT-L, Huang W-K, Chen Y, Chang H-M, Wang C-W. Induction of a cDNA clone from rice encoding a class II small heat shock protein by heat stress, mechanical injury, and salicylic acid. Plant Sci 2007, 172:64-75.
    • (2007) Plant Sci , vol.172 , pp. 64-75
    • Chang P-FL, J.T.-L.1    Huang, W.-K.2    Chen, Y.3    Chang, H.-M.4    Wang, C.-W.5
  • 62
    • 34247589657 scopus 로고    scopus 로고
    • Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants
    • 10.1111/j.1365-3040.2007.01664.x, 17470151
    • Saidi Y, Domini M, Choy F, Zryd JP, Schwitzguebel JP, Goloubinoff P. Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants. Plant Cell Environ 2007, 30:753-763. 10.1111/j.1365-3040.2007.01664.x, 17470151.
    • (2007) Plant Cell Environ , vol.30 , pp. 753-763
    • Saidi, Y.1    Domini, M.2    Choy, F.3    Zryd, J.P.4    Schwitzguebel, J.P.5    Goloubinoff, P.6
  • 63
    • 33748990885 scopus 로고    scopus 로고
    • Novel interrelationship between salicylic acid, abscisic acid, and PIP2-specific phospholipase C in heat acclimation-induced thermotolerance in pea leaves
    • 10.1093/jxb/erl098, 16908502
    • Liu H-T, Liu Y-Y, Pan Q-H, Yang H-R, Zhan J-C, Huang W-D. Novel interrelationship between salicylic acid, abscisic acid, and PIP2-specific phospholipase C in heat acclimation-induced thermotolerance in pea leaves. J Exp Bot 2006, 57:3337-3347. 10.1093/jxb/erl098, 16908502.
    • (2006) J Exp Bot , vol.57 , pp. 3337-3347
    • Liu, H.-T.1    Liu, Y.-Y.2    Pan, Q.-H.3    Yang, H.-R.4    Zhan, J.-C.5    Huang, W.-D.6
  • 65
    • 70349575248 scopus 로고    scopus 로고
    • Rice sHsp genes: genomic organization and expression profiling under stress and development
    • 10.1186/1471-2164-10-393, 2746236, 19703271
    • Sarkar N, Kim Y-K, Grover A. Rice sHsp genes: genomic organization and expression profiling under stress and development. BMC Genomics 2009, 10:393. 10.1186/1471-2164-10-393, 2746236, 19703271.
    • (2009) BMC Genomics , vol.10 , pp. 393
    • Sarkar, N.1    Kim, Y.-K.2    Grover, A.3
  • 66
    • 0003050958 scopus 로고
    • Photoinhibition of photosynthesis induced by visible light
    • Powles SB. Photoinhibition of photosynthesis induced by visible light. Annu Rev Plant Physiol 1984, 35:15-44.
    • (1984) Annu Rev Plant Physiol , vol.35 , pp. 15-44
    • Powles, S.B.1
  • 67
    • 80052396801 scopus 로고    scopus 로고
    • Small heat shock protein Hsp17.8 functions as an AKR2A cofactor in the targeting of chloroplast outer membrane proteins in Arabidopsis
    • 10.1104/pp.111.178681, 3165864, 21730198
    • Kim DH, Xu Z-Y, Na YJ, Yoo Y-J, Lee J, Sohn E-J, Hwang I. Small heat shock protein Hsp17.8 functions as an AKR2A cofactor in the targeting of chloroplast outer membrane proteins in Arabidopsis. Plant Physiol 2011, 157:132-146. 10.1104/pp.111.178681, 3165864, 21730198.
    • (2011) Plant Physiol , vol.157 , pp. 132-146
    • Kim, D.H.1    Xu, Z.-Y.2    Na, Y.J.3    Yoo, Y.-J.4    Lee, J.5    Sohn, E.-J.6    Hwang, I.7
  • 68
    • 80054746164 scopus 로고    scopus 로고
    • AlphaB-crystallin polydispersity is a consequence of unbiased quaternary dynamics
    • 10.1016/j.jmb.2011.07.016, 21839090
    • Baldwin AJ, Lioe H, Robinson CV, Kay LE, Benesch JL. alphaB-crystallin polydispersity is a consequence of unbiased quaternary dynamics. J Mol Biol 2011, 413:297-309. 10.1016/j.jmb.2011.07.016, 21839090.
    • (2011) J Mol Biol , vol.413 , pp. 297-309
    • Baldwin, A.J.1    Lioe, H.2    Robinson, C.V.3    Kay, L.E.4    Benesch, J.L.5
  • 69
    • 0025884282 scopus 로고
    • Stable transformation of the moss Physcomitrella patens
    • Schaefer D, Zryd JP, Knight CD, Cove DJ. Stable transformation of the moss Physcomitrella patens. Mol Gen Genet 1991, 226:418-424.
    • (1991) Mol Gen Genet , vol.226 , pp. 418-424
    • Schaefer, D.1    Zryd, J.P.2    Knight, C.D.3    Cove, D.J.4
  • 70
    • 0017404566 scopus 로고
    • The isolation and preliminary characterisation of auxotrophic and analogue resistant mutants of the moss, Physcomitrella patens
    • Ashton NW, Cove DJ. The isolation and preliminary characterisation of auxotrophic and analogue resistant mutants of the moss, Physcomitrella patens. Molec Gen Genet 1977, 154:87-95.
    • (1977) Molec Gen Genet , vol.154 , pp. 87-95
    • Ashton, N.W.1    Cove, D.J.2
  • 71
    • 0015914077 scopus 로고
    • Streptomycin resistant plants from callus culture of haploid tobacco
    • Maliga PBSZ, Marton L. Streptomycin resistant plants from callus culture of haploid tobacco. Nature 1973, 244:29-30.
    • (1973) Nature , vol.244 , pp. 29-30
    • Maliga, P.B.S.Z.1    Marton, L.2
  • 72
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • Murashige R, Skoog F. A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol Plant 1962, 15:473-497.
    • (1962) Physiol Plant , vol.15 , pp. 473-497
    • Murashige, R.1    Skoog, F.2
  • 75
    • 0036581417 scopus 로고    scopus 로고
    • GATEWAY vectors for Agrobacterium-mediated plant transformation
    • 10.1016/S1360-1385(02)02251-3, 11992820
    • Karimi M, Inze D, Depicker A. GATEWAY vectors for Agrobacterium-mediated plant transformation. Trends Plant Sci 2002, 7:193-195. 10.1016/S1360-1385(02)02251-3, 11992820.
    • (2002) Trends Plant Sci , vol.7 , pp. 193-195
    • Karimi, M.1    Inze, D.2    Depicker, A.3
  • 76
    • 0001200134 scopus 로고
    • The promoter of TL-DNA gene 5 controls the tissue-specific expression of chimaeric genes carried by a novel type of Agrobacterium binary vector
    • Koncz C, Schell J. The promoter of TL-DNA gene 5 controls the tissue-specific expression of chimaeric genes carried by a novel type of Agrobacterium binary vector. Molec Gen Genet 1986, 204:383-396.
    • (1986) Molec Gen Genet , vol.204 , pp. 383-396
    • Koncz, C.1    Schell, J.2
  • 77
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • 10.1046/j.1365-313x.1998.00343.x, 10069079
    • Clough SJ, Bent AF. Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 1998, 16:735-743. 10.1046/j.1365-313x.1998.00343.x, 10069079.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 78
    • 33749262307 scopus 로고    scopus 로고
    • Overexpression of the Arabidopsis syntaxin PEP12/SYP21 inhibits transport from the prevacuolar compartment to the lytic vacuole in vivo
    • 10.1105/tpc.105.040279, 1560924, 16935987
    • Foresti O, Da Silva LL, Denecke J. Overexpression of the Arabidopsis syntaxin PEP12/SYP21 inhibits transport from the prevacuolar compartment to the lytic vacuole in vivo. Plant Cell 2006, 18:2275-2293. 10.1105/tpc.105.040279, 1560924, 16935987.
    • (2006) Plant Cell , vol.18 , pp. 2275-2293
    • Foresti, O.1    Da Silva, L.L.2    Denecke, J.3
  • 79
    • 0141621588 scopus 로고    scopus 로고
    • The green fluorescent protein (GFP) as a reporter in plant cells
    • Oxford, UK: Oxford University Press, Hawes C, Satiat-Jeunemaitre B
    • Neuhaus J-M, Boevink P. The green fluorescent protein (GFP) as a reporter in plant cells. Plant Cell Biology 2001, 127-142. Oxford, UK: Oxford University Press, Hawes C, Satiat-Jeunemaitre B.
    • (2001) Plant Cell Biology , pp. 127-142
    • Neuhaus, J.-M.1    Boevink, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.