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Zoological Research
Kunming Institute of Zoology, Chinese Academy of Sciences
ISSN: 2095-8137
Vol. 26, No. 3, 2005, pp. 237-242
Bioline Code: zr05003
Full paper language: Chinese
Document type: Research Article
Document available free of charge

Zoological Research, Vol. 26, No. 3, 2005, pp. 237-242

 en Binding of the Zα Domain from a Carassius auratus check for this species in other resources 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

Abstract

Three fusion peptides,PZα1,PZα2 and PZα1Zα2 for Zα1 domain,Zα2 domain,and Zα1Zα2 domains of Carassius auratus check for this species in other resources 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.

Keywords
CaPKR-like protein kinase;Zα domain;Prokaryotic expression;Poly I:C binding;Dimerization

 
© Copyright 2005 Kunming Institute of Zoology, the Chinese Academy of Sciences
Alternative site location: http://www.zoores.ac.cn/

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