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Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33
Author(s) -
Wang Ying,
Han Ruifang,
Zhang Wanqi,
Yuan Yunfeng,
Zhang Xiaobin,
Long Yi,
Mi Huaifeng
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.01.055
Subject(s) - cyclophilin , rna , messenger rna , biochemistry , rna binding protein , chemistry , biology , microbiology and biotechnology , binding site , gene
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.