Virdi, A S and Thakur, A and Dutt, Som and Kumar, Sanjay and Singh, P (2009) A sorghum 85 kDa heat stress-modulated protein shows calmodulin-binding properties and cross-reactivity to anti-Neurospora crassa Hsp 80 antibodies. FEBS Letters, 583. pp. 767-770.
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Abstract
The present study, carried out to identify stress-modulated calmodulin (CaM)-binding proteins in sorghum, resulted in the isolation of several proteins, which showed binding to CaM-Sepharose matrix. Calmodulin gel overlay assay and MALDI-ToF MS analysis revealed that an 85 kDa protein (Hsp85), which interacted with calmodulin, cross-reacted with anti-N. crassa Hsp80 antibodies. Since these antibodies bind to plant Hsp90, sorghum Hsp85 is likely to be a member of the Hsp90 family. This study provides the first evidence that a member of Hsp90 (Hsp85) in plants exhibits CaM-binding properties. 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Item Type: | Article |
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Uncontrolled Keywords: | Calmodulin Calmodulin-binding protein Hsp Heat shock Sorghum |
Subjects: | Plant Biotechnology |
Divisions: | UNSPECIFIED |
Depositing User: | Dr. Aparna Maitra Pati |
Date Deposited: | 29 Dec 2011 15:52 |
Last Modified: | 06 Feb 2012 06:01 |
URI: | http://ihbt.csircentral.net/id/eprint/511 |
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