A sorghum 85 kDa heat stress-modulated protein shows calmodulin-binding properties and cross-reactivity to anti-Neurospora crassa Hsp 80 antibodies
IR@IHBT: CSIR-Institute of Himalayan Bioresource Technology, Palampur
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| Title |
A sorghum 85 kDa heat stress-modulated protein shows calmodulin-binding
properties and cross-reactivity to anti-Neurospora crassa Hsp 80 antibodies
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| Creator |
Virdi, A S
Thakur, A Dutt, Som Kumar, Sanjay Singh, P |
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| Subject |
Plant Biotechnology
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| Description |
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.
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| Date |
2009
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://ihbt.csircentral.net/511/1/308_2009_2%2D12%2D2011.pdf
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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| Relation |
http://ihbt.csircentral.net/511/
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