Three fusion peptides,P
Zα1,P
Zα2 and P
Zα1Zα2 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 P
Zα1Zα2 rather than P
Zα1,P
Zα2,and mixture of P
Zα1 and P
Zα2,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 P
Zα2 and P
Zα1Zα2 but a relative weak one for P
Zα1. 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.
