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.
Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33. Publishing Authors By Initials
Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33. Journal Published:
PUBLICATION TYPE: Journal Article
Journal: FEBS letters
VOLUME: 582
Page Numbers: 835-9
Journal Abbreviation: FEBS Lett.
ISSN: 0014-5793
DAY: 5
MONTH: 02
YEAR: 2008
Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33. Information
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LANGUAGE: eng
NlmUniqueID: 155157
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Grant and Affiliation Information for Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33.
AFFILIATION: Biochemical Section of Key Laboratory of Functional Polymer Materials, The Ministry of Education of China, Institute of Polymer Chemistry, Chemical School of Nankai University, 300071 Tianjin, PR China.
Country: Netherlands
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MEDLINETA: FEBS Lett
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