Interaction with Cu2+ disrupts the biological activity of glycine-rich protein GRP162

• 作 者: Xiaojian Qin Qi Huang Linlin Zhu Haijun Xiao Guoxin Yao Wenchao Huang Renshan Zhu Jun Hu Yingguo Zhu
• 机 构: State key laboratory of hybrid rice, College of Life Sciences, Wuhan University, Wuhan 430072, China
• 出 处: 第二届植物生物技术与现代农业论坛
• 发表日期: 2013年4期

The glycine-rich proteins (GRP) containing RNA recognition motifs (RRM) are involved in the regulation of transcriptional and/or post-transcriptional events.Previous studies have established that GRP162 plays an important role in the restoration of fertility in Honglian cytoplasmic male sterile (HL-CMS) rice.In this study, the ion binding properties of GRP162 were tested by isothermal titration calorimetry (ITC).The metal ions Cu2+ and Fe3+ bound GRP162, whereas Ca2+, Mn2+, Mg2+ and K+ did not.Furthermore, an electrophoretic mobility shift assay (EMSA) showed that interaction with Cu2+ interrupts the biological activity of GRP162 by disrupting the secondary structure of the protein.In contrast, Fe3+ did not impair the RNA binding ability of GRP162.The data suggest that Cu2+ in excess may disrupt RNA-binding proteins containing RRM that are essential for post-transcriptional regulation and may impair the development of plants or animals.