A temperature-responsive gene in sorghum encodes a glycine-rich protein that interacts with calmodulin.
Imposition of different biotic and abiotic stress conditions results in an increase in intracellular levels of Ca2+which is sensed by various sensor proteins. Calmodulin (CaM) is one of the best studied transducers of Ca2+signals. CaM undergoes conformational changes upon binding to Ca2+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 SbGRBP 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 Ca2+. 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.
Department of Biotechnology, Guru Nanak Dev University, Amritsar, 143005, Punjab, India.
Supreet
S
Singh
Department of Biotechnology, Guru Nanak Dev University, Amritsar, 143005, Punjab, India.
Amardeep Singh
AS
Virdi
Biotechnology Division, Institute of Himalayan Bioresource Technology, Palampur, 176061 Himachal Pradesh, India.
Rajdeep
R
Jaswal
Interdisciplinary Center for Plant Genomics and Department of Plant Molecular Biology, University of Delhi South Campus, New Delhi, 110021, India.
Mrinalini
M
Chawla
Interdisciplinary Center for Plant Genomics and Department of Plant Molecular Biology, University of Delhi South Campus, New Delhi, 110021, India.
Sanjay
S
Kapoor
Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, 600036, India.
Samar B
SB
Mohapatra
Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, 600036, India.
Narayanan
N
Manoj
Stress Physiology and Molecular Biology Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi, 110067, India.
Ashwani
A
Pareek
Biotechnology Division, Institute of Himalayan Bioresource Technology, Palampur, 176061 Himachal Pradesh, India. Electronic address: sanjayplp@rediffmail.com.
Sanjay
S
Kumar
Department of Biotechnology, Guru Nanak Dev University, Amritsar, 143005, Punjab, India. Electronic address: singhprabhjeet62@gmail.com.
Prabhjeet
P
Singh
D002118:Calcium; D002147:Calmodulin / Q000378:metabolism*; D002148:Calmodulin-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D018076:DNA, Complementary / Q000235:genetics; D018744:DNA, Plant; D018506:Gene Expression Regulation, Plant; D005998:Glycine / Q000737:chemistry*; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D045868:Sorghum / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D013696:Temperature
D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D018076:DNA, Complementary; D018744:DNA, Plant; D010940:Plant Proteins; D002118:Calcium; D005998:Glycine
Ca(2+); Calmodulin; Glycine-rich RNA-binding protein