HU Cheng-yu, XIE Zong-bo, ZHANG Yi-bing, CHEN Yu-dong, DENG Zheng-dong et al.. Binding of the Zα Domain from a Carassius auratus Protein Kinase PKR-like to Polyinosinic:Polycytidylic Acid. Zoological Research, 2005, 26(3): 237-242.
Citation:
HU Cheng-yu, XIE Zong-bo, ZHANG Yi-bing, CHEN Yu-dong, DENG Zheng-dong et al.. Binding of the Zα Domain from a Carassius auratus Protein Kinase PKR-like to Polyinosinic:Polycytidylic Acid. Zoological Research, 2005, 26(3): 237-242.
HU Cheng-yu, XIE Zong-bo, ZHANG Yi-bing, CHEN Yu-dong, DENG Zheng-dong et al.. Binding of the Zα Domain from a Carassius auratus Protein Kinase PKR-like to Polyinosinic:Polycytidylic Acid. Zoological Research, 2005, 26(3): 237-242.
Citation:
HU Cheng-yu, XIE Zong-bo, ZHANG Yi-bing, CHEN Yu-dong, DENG Zheng-dong et al.. Binding of the Zα Domain from a Carassius auratus Protein Kinase PKR-like to Polyinosinic:Polycytidylic Acid. Zoological Research, 2005, 26(3): 237-242.
Ecology and Biotechnology,Institute of Hydrobiology,the Chinese Academy of Sciences,Wuhan 430072,China 2.Chinese Academy of Sciences,Beijing 100039,China 3. Nanchang University,Nanchang 330047,China
Three fusion peptides,PZα1,PZα2 and PZα1Zα2 for Zα1 domain,Zα2 domain,and Zα1Zα2 domains of Carassius auratus PKR-like gene,respectively,were successfully expressed by a prokaryotic expression system and then purified by affinity chromatography. Gel mobility shift assay revealed that PZα1Zα2 rather than PZα1,PZα2,and mixture of PZα1 and PZα2,was capable to bind to polyinosinic∶polycytidylic acid (Poly I∶C) in vitro. In addition,all of the three fusion peptides all could form dimer,with strong dimerization for PZα2 and PZα1Zα2 but a relative weak one for PZα1. The results suggest that dsRNA, the by-product generated during virus replication in host cells,probably binds to the Zα domain of CaPKR-like and then regulates its physiological function.