메뉴 건너뛰기




Volumn 51, Issue 5, 2003, Pages 677-686

Heat-tolerant basmati rice engineered by over-expression of hsp101

Author keywords

Heat shock; Thermotolerance; Transgenic rice

Indexed keywords

CELLS; GROWTH KINETICS; HEAT RESISTANCE; HIGH TEMPERATURE EFFECTS; MOLECULAR WEIGHT; PROTEINS; STRESS ANALYSIS;

EID: 0037356546     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1022561926676     Document Type: Article
Times cited : (211)

References (45)
  • 1
    • 0032191255 scopus 로고    scopus 로고
    • Enhancement of the tolerance of Arabidopsis to high temperatures by genetic engineering of the synthesis of glycinebetaine
    • Alia, Hayashi, H., Sakamoto, A. and Murata, N. 1998. Enhancement of the tolerance of Arabidopsis to high temperatures by genetic engineering of the synthesis of glycinebetaine. Plant J. 16: 155-161.
    • (1998) Plant J. , vol.16 , pp. 155-161
    • Alia1    Hayashi, H.2    Sakamoto, A.3    Murata, N.4
  • 2
    • 0037342584 scopus 로고    scopus 로고
    • Molecular characterization of rice hsp101: Complementation of yeast hsp104 mutation by disaggregation of protein granules and differential expression in indica and japonica rice types
    • Agarwal, M., Sahi, C., Katiyar-Agarwal, S., Agarwal, S., Young, T., Gallie, D.R., Sharma, V., Ganesan, K. and Grover, A. 2002. Molecular characterization of rice hsp101: complementation of yeast hsp104 mutation by disaggregation of protein granules and differential expression in indica and japonica rice types. Plant Mol. Biol. 51: 541-551.
    • (2002) Plant Mol. Biol. , vol.51 , pp. 541-551
    • Agarwal, M.1    Sahi, C.2    Katiyar-Agarwal, S.3    Agarwal, S.4    Young, T.5    Gallie, D.R.6    Sharma, V.7    Ganesan, K.8    Grover, A.9
  • 3
    • 0012860512 scopus 로고    scopus 로고
    • Summing-up: Cutting-edge science for rice improvement-breakthroughs and beneficiaries
    • J. Goode and D. Chadwick (Eds.), Novartis Foundation/John Wiley, UK
    • Bennet, J. 2001. Summing-up: cutting-edge science for rice improvement-breakthroughs and beneficiaries. In: J. Goode and D. Chadwick (Eds.) Rice Biotechnology: Improving Yield, Stress Tolerance and Grain Quality, Novartis Foundation/John Wiley, UK, pp. 242-251.
    • (2001) Rice Biotechnology: Improving Yield, Stress Tolerance and Grain Quality , pp. 242-251
    • Bennet, J.1
  • 5
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidinium thiocyanate phenol chloroform extraction
    • Chomczynski, P. and Sacchi, N. 1987. Single step method of RNA isolation by acid guanidinium thiocyanate phenol chloroform extraction. Anal. Biochem. 162: 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 6
    • 0001510327 scopus 로고
    • Tissue specificity of the heat shock response in maize
    • Cooper, P., Ho, T.H.D. and Hauptmann, R.M. 1984. Tissue specificity of the heat shock response in maize. Plant Physiol. 75: 431-441.
    • (1984) Plant Physiol. , vol.75 , pp. 431-441
    • Cooper, P.1    Ho, T.H.D.2    Hauptmann, R.M.3
  • 9
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover, J.R. and Lindquist, S. 1998. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94: 73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 10
    • 0003110246 scopus 로고    scopus 로고
    • Towards production of abiotic stress tolerant transgenic rice plants: Issues, progress and future research needs
    • Grover, A. and Minhas, D. 2000. Towards production of abiotic stress tolerant transgenic rice plants: issues, progress and future research needs. Proc. Indian Natl. Acad. Sci. B66: 13-32.
    • (2000) Proc. Indian Natl. Acad. Sci. , vol.B66 , pp. 13-32
    • Grover, A.1    Minhas, D.2
  • 11
    • 0034636040 scopus 로고    scopus 로고
    • Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress
    • Hong, S.W. and Vierling, E. 2000. Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress. Proc. Natl. Acad. Sci. USA 97: 4392-4397.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4392-4397
    • Hong, S.W.1    Vierling, E.2
  • 13
    • 0012864064 scopus 로고    scopus 로고
    • Binary cloning vectors for efficient genetic transformation of rice
    • Katiyar-Agarwal, S., Kapoor, A. and Grover, A. 2002. Binary cloning vectors for efficient genetic transformation of rice. Curr. Sci. 82: 873-876.
    • (2002) Curr. Sci. , vol.82 , pp. 873-876
    • Katiyar-Agarwal, S.1    Kapoor, A.2    Grover, A.3
  • 15
    • 0004098281 scopus 로고
    • International Rice Research Institute, Manila/CAB International, UK
    • Khush, G.S. and Toenniessen, G.H. 1991. Rice Biotechnology. International Rice Research Institute, Manila/CAB International, UK.
    • (1991) Rice Biotechnology
    • Khush, G.S.1    Toenniessen, G.H.2
  • 16
    • 0028675574 scopus 로고
    • A soyabean 101-KD heat shock protein complements yeast HSP 104 deletion mutant in acquiring thermotolerance
    • Lee, Y.J., Nagao, R.T. and Key, J.L. 1994. A soyabean 101-KD heat shock protein complements yeast HSP 104 deletion mutant in acquiring thermotolerance. Plant Cell 6: 1889-1897.
    • (1994) Plant Cell , vol.6 , pp. 1889-1897
    • Lee, Y.J.1    Nagao, R.T.2    Key, J.L.3
  • 17
    • 0028883383 scopus 로고
    • Cloning and characterization of a cDNA encoding an 18.0-kDa class-I low-molecular weight heat-shock protein from rice
    • Lee, Y.L., Chang, P.L., Yeh, K.W., Jinn, T.L., Kung, C.S., Lin, W.C., Cehn, Y.M. and Lin, C.Y. 1995. Cloning and characterization of a cDNA encoding an 18.0-kDa class-I low-molecular weight heat-shock protein from rice. Gene 165: 223-227.
    • (1995) Gene , vol.165 , pp. 223-227
    • Lee, Y.L.1    Chang, P.L.2    Yeh, K.W.3    Jinn, T.L.4    Kung, C.S.5    Lin, W.C.6    Cehn, Y.M.7    Lin, C.Y.8
  • 18
    • 0029379547 scopus 로고
    • Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis
    • Lee, J.H., Hubel, A. and Schoffi, F. 1995. Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis. Plant J. 8: 603-612.
    • (1995) Plant J. , vol.8 , pp. 603-612
    • Lee, J.H.1    Hubel, A.2    Schoffi, F.3
  • 19
    • 0033877118 scopus 로고    scopus 로고
    • Heat shock protein, HSP101, binds to the Fed-1 internal light regulatory element and mediates its high translational activity
    • Ling, J., Wells, D.R., Tanguay, R.L., Dickey, L.F., Thompson, W.F. and Gallie, D.R. 2000. Heat shock protein, HSP101, binds to the Fed-1 internal light regulatory element and mediates its high translational activity. Plant Cell 12: 1213-1227.
    • (2000) Plant Cell , vol.12 , pp. 1213-1227
    • Ling, J.1    Wells, D.R.2    Tanguay, R.L.3    Dickey, L.F.4    Thompson, W.F.5    Gallie, D.R.6
  • 20
    • 0032697142 scopus 로고    scopus 로고
    • Modified expression of a carrot small heat shock protein gene, Hsp17.7, results in increased or decreased thermotolerance
    • Malik, M.K., Slovin, J.P., Hwang, C.H. and Zimmerman, J.L. 1999. Modified expression of a carrot small heat shock protein gene, Hsp17.7, results in increased or decreased thermotolerance. Plant J. 20: 89-99.
    • (1999) Plant J. , vol.20 , pp. 89-99
    • Malik, M.K.1    Slovin, J.P.2    Hwang, C.H.3    Zimmerman, J.L.4
  • 21
    • 0034695494 scopus 로고    scopus 로고
    • Trienoic fatty acids and plant tolerance of high temperature
    • Murakami, Y., Tsuyama, M., Kobayashi, Y. and Kodama, H. 2000. Trienoic fatty acids and plant tolerance of high temperature. Science 287: 476-479.
    • (2000) Science , vol.287 , pp. 476-479
    • Murakami, Y.1    Tsuyama, M.2    Kobayashi, Y.3    Kodama, H.4
  • 22
    • 0012816620 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • Murashige, T. and Skoog, F. 1962. A revised medium for rapid growth and bioassays with tobacco tissue cultures. Planta 157: 385-391.
    • (1962) Planta , vol.157 , pp. 385-391
    • Murashige, T.1    Skoog, F.2
  • 23
    • 0030175179 scopus 로고    scopus 로고
    • Effects of light and temperature on expression of Clp C, the regulatory subunit of chloroplastic Clp protease, in pea seedlings
    • Ostersetzer, O. and Adam, Z. 1996. Effects of light and temperature on expression of Clp C, the regulatory subunit of chloroplastic Clp protease, in pea seedlings. Plant Mol. Biol. 31: 673-676.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 673-676
    • Ostersetzer, O.1    Adam, Z.2
  • 24
    • 0029947569 scopus 로고    scopus 로고
    • Immunological detection of proteins similar to bacterial proteases in higher plant chloroplasts
    • Ostersetzer, O., Tabak, S., Yarden, O., Shapira, R. and Adam, Z. 1996. Immunological detection of proteins similar to bacterial proteases in higher plant chloroplasts. Eur. J. Biochem. 236: 932-936.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 932-936
    • Ostersetzer, O.1    Tabak, S.2    Yarden, O.3    Shapira, R.4    Adam, Z.5
  • 25
    • 0029379740 scopus 로고
    • Immunological evidence for accumulation of two novel 104 and 90 kDa HSPs in response to diverse stresses in rice and in response to high temperature stress in diverse plant genera
    • Pareek, A., Singla, S.L. and Grover, A. 1995. Immunological evidence for accumulation of two novel 104 and 90 kDa HSPs in response to diverse stresses in rice and in response to high temperature stress in diverse plant genera. Plant Mol. Biol. 29: 293-300.
    • (1995) Plant Mol. Biol. , vol.29 , pp. 293-300
    • Pareek, A.1    Singla, S.L.2    Grover, A.3
  • 26
    • 0000735772 scopus 로고    scopus 로고
    • Protein alterations associated with salinity, desiccation, high and low temperature stresses and abscisic acid application in seedlings of Pusa 169, a high-yielding rice (Oryza sativa L.) cultivar
    • Pareek, A., Singla, S.L. and Grover, A. 1998. Protein alterations associated with salinity, desiccation, high and low temperature stresses and abscisic acid application in seedlings of Pusa 169, a high-yielding rice (Oryza sativa L.) cultivar. Curr. Sci. 75: 1023-1035.
    • (1998) Curr. Sci. , vol.75 , pp. 1023-1035
    • Pareek, A.1    Singla, S.L.2    Grover, A.3
  • 27
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp 104
    • Parsell, D.A., Kowal, A.S., Singer, M.A. and Lindquist, S. 1994. Protein disaggregation mediated by heat-shock protein Hsp 104. Nature 372: 475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 28
    • 0034119621 scopus 로고    scopus 로고
    • Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis
    • Queitsch, C., Hong, S.W., Vierling, E. and Lindquist, S. 2000. Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis. Plant Cell 12: 479-492.
    • (2000) Plant Cell , vol.12 , pp. 479-492
    • Queitsch, C.1    Hong, S.W.2    Vierling, E.3    Lindquist, S.4
  • 30
    • 84996416221 scopus 로고
    • High temperature induced sterility in indica rice at flowering
    • Satake, T. and Yoshida, S. 1978. High temperature induced sterility in indica rice at flowering. J. Crop Sci. 447: 6-17.
    • (1978) J. Crop Sci. , vol.447 , pp. 6-17
    • Satake, T.1    Yoshida, S.2
  • 31
    • 0028675582 scopus 로고
    • An Arabidopsis heat shock protein complements a thermotolerance defect in yeast
    • Schirmer, E.C., Lindquist, S. and Vierling, E. 1994. An Arabidopsis heat shock protein complements a thermotolerance defect in yeast. Plant Cell 6: 1899-1909.
    • (1994) Plant Cell , vol.6 , pp. 1899-1909
    • Schirmer, E.C.1    Lindquist, S.2    Vierling, E.3
  • 32
    • 0029392885 scopus 로고
    • The stroma of higher plant plastids contain Clp P and Clp C, functional homologs of Escherichia coli Clp P and Clp A: An archetypal two-component ATP-dependent protease
    • Shanklin, J., Dewitt, N.D. and Flanagan, J.M. 1995. The stroma of higher plant plastids contain Clp P and Clp C, functional homologs of Escherichia coli Clp P and Clp A: an archetypal two-component ATP-dependent protease. Plant Cell 7: 1713-1722.
    • (1995) Plant Cell , vol.7 , pp. 1713-1722
    • Shanklin, J.1    Dewitt, N.D.2    Flanagan, J.M.3
  • 33
    • 0027661698 scopus 로고
    • Antibodies raised against a yeast heat shock protein cross-react with a heat and abscisic acid-regulated polypeptide in rice
    • Singla, S.L. and Grover, A., 1993. Antibodies raised against a yeast heat shock protein cross-react with a heat and abscisic acid-regulated polypeptide in rice. Plant Mol. Biol. 22: 1177-1180.
    • (1993) Plant Mol. Biol. , vol.22 , pp. 1177-1180
    • Singla, S.L.1    Grover, A.2
  • 34
    • 0028045339 scopus 로고
    • Detection and quantitation of a rapidly accumulating and predominant 104kDa heat shock polypeptide in rice
    • Singla, S.L. and Grover, A. 1994. Detection and quantitation of a rapidly accumulating and predominant 104kDa heat shock polypeptide in rice. Plant Sci. 97: 23-30.
    • (1994) Plant Sci. , vol.97 , pp. 23-30
    • Singla, S.L.1    Grover, A.2
  • 35
    • 0001405194 scopus 로고    scopus 로고
    • High temperature
    • M.N.V. Prasad (Ed.), John Wiley, New York
    • Singla, S. L., Pareek, A. and Grover, A. 1997a. High temperature. In: M.N.V. Prasad (Ed.) Plant Ecophysiology, John Wiley, New York, pp. 101-127.
    • (1997) Plant Ecophysiology , pp. 101-127
    • Singla, S.L.1    Pareek, A.2    Grover, A.3
  • 36
    • 0031591583 scopus 로고    scopus 로고
    • Yeast HSP104 homologue rice HSP110 is developmentally- and stress-regulated
    • Singla, S.L., Pareek, A. and Grover, A. 1997b. Yeast HSP104 homologue rice HSP110 is developmentally- and stress-regulated. Plant Sci. 125: 211-219.
    • (1997) Plant Sci. , vol.125 , pp. 211-219
    • Singla, S.L.1    Pareek, A.2    Grover, A.3
  • 37
    • 0031760059 scopus 로고    scopus 로고
    • Plant HSP100 family with special reference to rice
    • Singla S.L., Pareek, A. and Grover, A. 1998a. Plant HSP100 family with special reference to rice. J. Biosci. 23: 337-345.
    • (1998) J. Biosci. , vol.23 , pp. 337-345
    • Singla, S.L.1    Pareek, A.2    Grover, A.3
  • 38
    • 0032145547 scopus 로고    scopus 로고
    • Distribution patterns of 104 kDa stress-associated protein of rice reveal its constitutive accumulation in seeds and disappearance from the just-emerged seedlings
    • Singla, S.L., Pareek, A. and Grover, A. 1998b. Distribution patterns of 104 kDa stress-associated protein of rice reveal its constitutive accumulation in seeds and disappearance from the just-emerged seedlings. Plant Mol. Biol. 37: 911-919.
    • (1998) Plant Mol. Biol. , vol.37 , pp. 911-919
    • Singla, S.L.1    Pareek, A.2    Grover, A.3
  • 39
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76: 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 41
    • 0031397444 scopus 로고    scopus 로고
    • Intron-mediated improvement of a selectable marker gene for plant transformation using Agrobacterium tumefaciens
    • Wang, M.B., Upadhyaya, N.M., Brettell, R.I.S. and Waterhouse, P.M. 1997. Intron-mediated improvement of a selectable marker gene for plant transformation using Agrobacterium tumefaciens. J. Genet. Breed. 51: 325-334.
    • (1997) J. Genet. Breed. , vol.51 , pp. 325-334
    • Wang, M.B.1    Upadhyaya, N.M.2    Brettell, R.I.S.3    Waterhouse, P.M.4
  • 42
    • 0032532127 scopus 로고    scopus 로고
    • HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status
    • Wells, D.R., Tanguay, R.L., Le, H. and Gallie, D.R. 1998. HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status. Genes Dev. 12: 3236-3251.
    • (1998) Genes Dev. , vol.12 , pp. 3236-3251
    • Wells, D.R.1    Tanguay, R.L.2    Le, H.3    Gallie, D.R.4
  • 43
    • 0030886055 scopus 로고    scopus 로고
    • Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance
    • Yeh C.H., Yeh, K.W., Wu, S.H., Chang, P.L., Chen, Y.M. and Lin, C.Y. 1997. Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance. Proc. Natl. Acad. Sci. USA 94: 10967-10972.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10967-10972
    • Yeh, C.H.1    Yeh, K.W.2    Wu, S.H.3    Chang, P.L.4    Chen, Y.M.5    Lin, C.Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.