Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051190 | FEBS Letters | 2008 | 5 Pages |
Abstract
Human nuclear cyclophilin 33 (hCyP33) was the first protein which was found to contain an RNA-binding motif and a PPIase domain. It was not known what cellular and physiological roles are played by the RNA-binding activity as well as the PPIase activity of hCyP33. In this paper, we investigated the binding specificity of hCyP33 to different cellular RNA using ion-exchange chromatography and affinity adsorption. Furthermore, the influence of different cellular RNAs to the PPIase activity of hCyP33 was investigated using a protease-coupled method. The results show that hCyP33 binds specifically to mRNA, namely poly(A)+RNA, and that binding stimulates the PPIase activity of hCyP33.
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Authors
Ying Wang, Ruifang Han, Wanqi Zhang, Yunfeng Yuan, Xiaobin Zhang, Yi Long, Huaifeng Mi,