A sorghum 85kDa heat stress-modulated protein shows calmodulin-binding properties and cross-reactivity to anti-Neurospora crassa Hsp 80 antibodies.
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 85kDa 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.
Virdi
Amardeep Singh
AS
Department of Biotechnology, Guru Nanak Dev University, Amritsar, Punjab 143005, India.
Thakur
Aditi
A
Dutt
Som
S
Kumar
Sanjay
S
Singh
Prabhjeet
P
D000906:Antibodies / Q000378:metabolism*; D002147:Calmodulin / Q000302:isolation & purification / Q000378:metabolism*; D003429:Cross Reactions; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D008970:Molecular Weight; D009492:Neurospora crassa / Q000378:metabolism*; D011485:Protein Binding; D045868:Sorghum / Q000378:metabolism*
D000906:Antibodies; D002147:Calmodulin; D006360:Heat-Shock Proteins