Human cyclophilin 33 (hCyP33) in T-cell binds specifically to poly(A)^+RNA (mRNA)

作     者：张万起 袁直 宓怀风 元云峰 何炳林 王亦农 

作者机构：1. State Key Laboratory of Functional Polymer Materials for Adsorption and Separation Institute of Polymer Chemistry Nankai University 300071 Tianjin China 

出 版 物：《Science China Chemistry》 (中国科学（化学英文版）)

年 卷 期：2002年第45卷第3期

页      面：275-281页

核心收录：

学科分类：1001[医学-基础医学(可授医学、理学学位)] 10[医学] 

基　　金：This work was supported by the State Key Fundamental R & D Project (Grant No. G1999064707) Ministry of Education of China (Department of Foreign Affairs (99)747) German World University Service 

主　　题：human cyclophilin 33 (hCyP33) ion-exchange chromatography RNA-binding specificity. 

摘      要：Human cyclophilin 33 (hCyP33), found in 1996, consists of an RNA-binding domain in N-terminus, a cyclophilin domain in C-terminus and a connected part between the two domains. RNA-binding proteins concern functions, such as splicing, modification and transport, after transcription in eukaryotic cells. Cyclophilins (CyPs) possess enzymatic activity, namely peptidyl-proryl cis-trans isomerase (PPIase). They are involved in folding, transport and interaction of proteins. Cyclosporin A (CsA), an immunosuppressant used by organ transplantation, binds to CyPs and suppresses their enzymatic activity. However, up to now it is unknown that which cellular and physiological roles hCyP33, which possesses the above-mentioned both functions, plays. In this paper the binding specificity of hCyP33 to different cellular RNA is investigated by means of ion-exchange chromatography and affinity adsorption. The results show that it binds specifically to poly(A) tailed mRNA, namely poly(A)+RNA.