Journal of Stress Physiology &
Biochemistry, Vol. 9 No. 1
2013, pp. 74-86 ISSN 1997-0838
Original Text Copyright (cc) 2013 by Nagesh Babu, Balaji and Devaraj
ORIGINAL
ARTICLE
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QueryDate : 2016-12-24
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Purification, characterization
and partial cDNA cloning of high-temperature stress-induced protein
from French bean (Phaseolus vulgaris)
Nagesh Babu R.*1, Balaji
K.N.2 and Devaraj V.R.3 1 Post Graduate Department of Biochemistry,
Maharani’s Science College for Women, Bangalore-560001 INDIA 2 Department of Microbiology Cell Biology, Indian Institute
of Science, Bangalore-560012, INDIA 3 Department of Biochemistry, Central College Campus,
Bangalore University, Bangalore-560001, INDIA
*E-Mail: nageshbabur@gmail.com
Received September 27, 2012
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.
