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Updated: Jul 7, 2026

Novel RNA-Binding Proteins Isolation by the RaPID Methodology
Published on: September 30, 2016
Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33
Ying Wang1, Ruifang Han, Wanqi Zhang
1Biochemical Section of Key Laboratory of Functional Polymer Materials, The Ministry of Education of China, Institute of Polymer Chemistry, Chemical School of Nankai University, Tianjin, PR China.
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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