On July 24, Cell Research published the research results of Liu Yingfang's research group at the Institute of Biophysics, Chinese Academy of Sciences, entitled Crystal structure of ISG54 reveals a novel RNA binding structure and potential functional mechanisms. This achievement is another new development in the research group of Liu Yingfang's group following the research work on the antiviral protein ZAP (NSMB. 2012 Mar 11; 19 (4): 430-5), in the structure and function of interferon-induced antiviral protein.
Members of the Interferon-stimulated gene 56, ISG56 family play an important role in cells' resistance to viral invasion, but their functional mechanism has been unclear. Early reports suggested that ISG54 and ISG56 family members can perform antiviral functions by inhibiting the formation of translation initiation complexes. It was later discovered that members of this family also affect the expression of cytokines. Recent research results have shown that ISG54 and ISG56 can recognize non-host mRNA to exercise antiviral functions. Although these results provide a possible mechanism for the antiviral function of ISG56 family members, they cannot explain the mechanism of cell function.
Liu Yingfang's group analyzed the crystal structure and found that ISG54 has a brand-new RNA-binding protein structure, which contains 9 tetratricopeptide repeat-like domains, forming domain-swapped disosomes (Figure). The C-terminal of ISG54 folds into a supercoiled structure that can be used to bind viral mRNA. After the key residues of these RNA binding sites are mutated, ISG54 will lose its RNA binding ability and antiviral function.
It was also unexpectedly found in the study that ISG54 has a strong selectivity for RNA sequences, and it tends to bind AU-rich RNA, which does not depend on the characteristics of mRNA Cap and 5 'triphosphorylation. Further research shows that ISG54 can bind to the ARE sequence of the non-coding region of cytokine protein mRNA. Because ARE plays an important role in regulating the stability of mRNA, the researchers speculate that this may be the key to ISG54's cell function.
As the first structure of ISG56 family proteins, this work is of great significance for explaining the functional mechanism of ISG56 family members.
This work was completed by researcher Liu Yingfang and Academician Shu Hongbing of Wuhan University. The research project was supported by the Ministry of Science and Technology, the National Natural Science Foundation of China and the Chinese Academy of Sciences, as well as the support of Shanghai Light Source and Diamond Synchrotron Radiation Light Source.
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