2. Academic Validation
  3. Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33

Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33

  • FEBS Lett. 2008 Mar 5;582(5):835-9. doi: 10.1016/j.febslet.2008.01.055.
Ying Wang 1,  Ruifang Han,  Wanqi Zhang,  Yunfeng Yuan,  Xiaobin Zhang,  Yi Long,  Huaifeng Mi
Affiliations

Affiliation

  • 1 Biochemical 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.
PMID: 18258190 DOI: 10.1016/j.febslet.2008.01.055
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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