Imposition of different biotic and abiotic stress conditions results in an increase in intracellular levels of Ca
which is sensed by various sensor proteins. Calmodulin (CaM) is one of the best studied transducers of Ca
signals. CaM undergoes conformational changes upon binding to Ca
and interacts with different types of proteins, thereby, regulating their activities. The present study reports the cloning and characterization of a sorghum cDNA encoding a protein (SbGRBP) that shows homology to glycine-rich RNA-binding proteins. The expression of
in the sorghum seedlings is modulated by heat stress. The SbGRBP protein is localized in the nucleus as well as in cytosol, and shows interaction with CaM that requires the presence of Ca
. SbGRBP depicts binding to single- and also double-stranded DNA. Fluorescence spectroscopic analyses suggest that interaction of SbGRBP with nucleic acids may be modulated after binding with CaM. To our knowledge, this is the first study to provide evidence for interaction of a stress regulated glycine-rich RNA-binding protein with CaM.
• cDNA encoding a Sorghum glycine-rich RNA-binding protein (SbGRBP) has been cloned.
• SbGRBP shows interaction with CaM, which is Ca
• First study to demonstrate interaction of CaM with a protein of GRBP family.
• SbGRBP also shows binding with single- and double stranded DNA.
• Interaction of SbGRBP with DNA appears to be modulated by CaM.
The preview is over
If you wish to continue, please create your membership or