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ISSN 0582-9879 Acta Biochim et Biophysica Sinica 2004, 36(3):169-176 CN 31-1300/Q
Cinnamomin
–a Versatile Type II Ribosome-inactivating Protein
Hong XU and Wang-Yi
LIU*
( State Key Laboratory of Molecular Biology, the Institute of Biochemistry and
Cell Biology, Shanghai Institutes for Biological Sciences,
the Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China )
Abstract Ribosome-inactivating proteins (RIPs) are a group of toxic proteins that can specifically act on the universally conserved sarcin/ricin domain (S/R domain) of the largest RNA in ribosome and thus irreversibly inactivate ribosome for protein synthesis. Cinnamomin is a multifunctional type II RIP isolated in our laboratory from the mature seeds of the camphor tree. This protein has been extensively studied with regard to its purification, characteristics, structure and function, genetic expression, enzymatic mechanism, physiological role in seed cell and toxicity to cancer cells and insect larvae. The research results of cinnamomin obtained in our laboratory are summarized in this review. Understanding of cinnamomin and the relative new proteins will help expand our knowledge of RIPs and may accelerate theoretical study and the development of their potential applications.
Key words cinnamomin; cinphorin;
ribosome-inactivating protein
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Received: October 14, 2003 Accepted:
January 3, 2004
*Corresponding author: Tel, 86-21-54921238; Fax, 86-21-54921011; E-mail, [email protected]