Purification, characterization and partial cDNA cloning of hightemperature stress-induced protein from French bean ( Phaseolus vulgaris)

Автор: Nagesh Babu R, Balaji K.N., Devaraj V.R.

Журнал: Журнал стресс-физиологии и биохимии @jspb

Статья в выпуске: 1 т.9, 2013 года.

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In order to identify the components of high temperature response in French bean, three heat shock proteins induced under high temperature were purified to homogeneity by Carboxy methyl cellulose and sephadex G-100 chromatography followed by preparative SDS-PAGE. Two of these, Hsp1 and Hsp3 were further characterized by immuno-detection with polyclonal antibodies. Hsp3 exhibited ATPase and chaperone activity with malate dehydrogenase and citrate synthase. Partial cDNA for Hsp3 synthesized using the primer derived from amino-terminal sequence was cloned and expressed in Escherichia coli. The recombinant protein possesses ATPase activity, and showed thermal protection at 50°C in Escherichia coli. The translated partial cDNA showed homology with stress induced proteins including ATPases from higher plants. These results supported the fact that French bean response to high temperature stress involves Hsps as one of the principal components.

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Cdna, french bean, hts, hsps

Короткий адрес: https://sciup.org/14323725

IDR: 14323725

Список литературы Purification, characterization and partial cDNA cloning of hightemperature stress-induced protein from French bean ( Phaseolus vulgaris)

  • Ashraf M. (2010) Inducing drought tolerance in plants. Recent advances Biotechnology Advances. 28: 169-183.
  • Bradford M.M. (1976) A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72: 248-254.
  • Chan K.M., Delfert D., Junger K.D. (1986) A direct colorimetric assay for Ca2+-stimulated ATPase activity. Analytical Biochemistry. 157(2): 375-380.
  • Cho K., Song J.B. (2007) ATP-independent thermo-protective activity of Nicotiana tabacum heat shock protein 70 in E. coli. J. Biochem and Mol Biol. 40: 107-112.
  • Gerold Beckers J.M., Jaskiewicz M., Liu Y., William R., Sheng U., He Y., Zhang S., and Conratha U. (2009) Mitogen-activated protein kinases 3 and 6 are required for full priming of stress responses in Arabidopsis thaliana. The Plant Cell. 21(3): 944-953
  • Green P.J. (1993) Control of mRNA stability in higher plants. Plant Physiol. 102: 1065-1070.
  • Guy C., Kaplan F., Kopka J., Selbig J. and Hincha D.K. (2008) Metabolomics of temperature stress, Physiologia Plantarum. 132(2): 220-235.
  • Hall A.E. (2001) Crop Responses to Environment. CRC Press, LLC, Boca. Raton Florida
  • Huang B. and Xu C. (2008) Identification and characterization of proteins associated with plant tolerance to heat stress. Journal of Integrative Plant Biology. 50(10): 1230-1237.
  • Ito Y., Karsura K., Maruyama K., Taji T., Kobayashi M., Seki M.M, Shinozaki K, Yamaguchi-Shinozaki K. (2006) Functional analysis of rice DREB/CBF-type transcription factors involved in cold-responsive Gene expression in transgenic Rice. Plant and Cell Physiol. 47: 141-153.
  • Jagadish S.V.K., Muthurajan R., Oane R., Wheeler T. R., Heuer S., Bennett J. and Craufurd P.Q, (2010) Physiological and proteomic approaches to address heat tolerance during anthesis in rice (Oryza sativa L.). Journal of Experimental Botany. 61: 143-156.
  • Katiyar-Agarwal S., Agarwal M., Grover A., (2003) Heat-tolerant basmati rice engineered by over-expression of hsp101. Plant Mol Biol. 51: 677-686.
  • Laemmli U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227: 680-686.
  • Lee G., Pokala N., Vierling E. (1995) Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea. J. Biol Chem. 270: 10432-10438.
  • Liberek K., Lewandowska A., Zietkiewicz S. (2008) Chaperones in control of protein disaggregation. EMBO J. 27(2): 328-335.
  • Nagesh Babu R., Devaraj V.R. (2008) High temperature and salt stress response in French bean (Phaseolus vulgaris). Australian Journal of Crop Science. 2(2): 40-48.
  • Porter J.R. (2005) Rising temperatures is likely to reduce crop yields. Nature. 436: 174-179.
  • Sachin K., Larkindale J., Lee U., Koskull P., Vierling D.E. and Scharf K.D. (2007) Complexity of the heat stress response in plants. Current Opinion in Plant Biology. 10(3): 310-316.
  • Seki M., Narusaka M., Ishida J., Nanjo T., Fujita M., Oono Y., Kamiya A., Nakajima M., Enju A., Sakurai T. (2002) Monitoring the expression profiles of 7000 Arabidopsis genes under drought, cold and high-salinity stresses using a full-length cDNA microarray. Plant J. 31: 279-292.
  • Sere P.A., Brazil H., Gonen L. (1963) The citrate condensing enzyme of pigeon breast muscle and moth flight muscle. Acta chem. Scand. 17: 129-134.
  • Shinozaki K., and Yamaguchi-Shinozaki K. (2006) Transcriptional regulatory networks in cellular responses and tolerance to dehydration and cold stress. Annual Review of Plant Biology 57: 781-803.
  • Singh A., Grover A. (2008) Genetic engineering for heat tolerance in plants. Physiol. Mol. Biol. Plants. 14: 155-165.
  • Vidal V., Ranty B., Dillenschneider M., Charpenteau M., Ranjeva R. (1993) Molecular characterization of a 70 k Da heat shock proteins of bean mitochondria. Plant J. 3: 143-150
  • Vierling E. (1991) The heat shock response in plants. Annu Rev Plant Physiol Plant Mol Biol. 42: 579-620.
  • Wahid A., Gelani S., Ashraf M., Foolad M.R. (2007) Heat tolerance in plants: An overview. Environmental and Experimental Botany. 61: 199-223.
  • Wang, W., Vinocur, B., Shoseyov, O., Altman, A. (2004) The role of plant heat-shock proteins/molecular chaperones in the abiotic stress response. Trends in Plant Science 9(5): 244-252.
  • Young T.E., Ling J., Geisler-Lee C.J., Tanguay R.L., Caldwell C., Gallie D.R. (2001) Developmental and thermal regulation of maize heat shock protein, Hsp101. Plant Physiol. 127: 777-791.
  • Zhang Z.L., Zhu J.H., Zhan Q.I., Cai Y.B. (2009) Molecular characterization of an ethephon-induced Hsp70 involved in high and low-temperature responses in Hevea brasiliensis. Plant Physiology and Biochemistry. 47: 954-959.
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