Three fusion peptides, P-Z alpha 1, P-Z alpha 2 and P-Z alpha 1Z alpha 2 for Z alpha 1 domain, Z alpha 2 domain, and Z alpha 1Z alpha 2 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 P-Z alpha 1Z alpha 2 rather than P-Z alpha 1, P-Z alpha 2, and mixture of P-Z alpha 1 and P-Z alpha 2, was capable to bind to polyinosinic: polycytidylic acid (Poly 1: C) in vitro. In addition, all of the three fusion peptides all could form dimer, with strong dimerization for P-Z alpha 2 and P-Z alpha 1Z alpha 2 but a relative weak one for P-Z alpha 1. The results suggest that dsRNA, the by-product generated during virus replication in host cells, probably binds to the Z alpha domain of CaPKR-like and then regulates its physiological function.
Hu Cheng-yu; Xie Zong-bo; Zhang Yi-bing; Chen Yu-dong; Deng Zheng-dong; Jiang Jun; Gui Jian-fang (email@example.com).Binding of the Z alpha domain from a Carassius auratus protein kinase PKR-like to polyinosinic:polycytidylic acid,Zoological Research,2005,26(3):237-242