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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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
Uncontrolled Keywords: Calmodulin Calmodulin-binding protein Hsp Heat shock Sorghum
Subjects: Plant Biotechnology
Depositing User: Dr. Aparna Maitra Pati
Date Deposited: 29 Dec 2011 15:52
Last Modified: 06 Feb 2012 06:01

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