Binding of the Zα Domain from a Carassius auratus Protein Kinase PKR-like to Polyinosinic:Polycytidylic Acid

HU Cheng-yu; XIE Zong-bo; ZHANG Yi-bing; CHEN Yu-dong; DENG Zheng-dong et al.

Volume 26 Issue 3

May 2005

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Article Navigation > 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.

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Binding of the Zα Domain from a Carassius auratus Protein Kinase PKR-like to Polyinosinic:Polycytidylic Acid

1.
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

Received Date: 1900-01-01
Rev Recd Date: 1900-01-01
Publish Date: 2005-06-22

Abstract

Abstract

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.
- CaPKR-like protein kinase,
- Zα domain,
- Prokaryotic expression,
- Poly I∶C binding,
- Dimerization