| 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.
Keywords
												
											Related Topics
												
													Life Sciences
													Agricultural and Biological Sciences
													Plant Science
												
											Authors
												Ying Wang, Ruifang Han, Wanqi Zhang, Yunfeng Yuan, Xiaobin Zhang, Yi Long, Huaifeng Mi, 
											