The scientific journal Nature Structural & Molecular Biology published online a paper entitled “EF-G catalyzes tRNA translocation by disrupting interactions between decoding center and codon–anticodon duplex” on August 10th, 2014 reported a breakthrough in ribosomal functional study conducted by Professor QIN Yan’s laboratory of RNA biology at the Institute of Biophysics, Chinese Academy of Sciences.

Ribosome is protein translation factory. In the process of translation, elongation factor G (EF-G) plays an essential role in catalyzing the ribosome moving along the mRNA constantly, thus for a complete protein biosynthesis. How EF-G initiates ribosome translocation is a key question which is still unsolved.

Professor QIN Yan and her colleagues performed systematic mutagenesis of EF-G and found that the interactions between the decoding center and the codon–anticodon duplex constitute the barrier for translocation. Catalysis of translocation by EF-G involves the factor’s highly conserved loops I and II at the tip of domain IV, which disrupt the hydrogen bonds between the decoding center and the duplex to release the latter, hence inducing subsequent translocation events (Fig. 1).

Over the years, QIN’s team has been engaged in the research of ribosomal translocation mechanism. This work is significant not only in this field but also a breakthrough in the experimental methodology. The theoretical basis provided by this study may lead to the development of new antibiotics.

The work was supported by grants from the Ministry of Science and Technology of China, the Chinese Academy of Sciences and the National Natural Science Foundation of China.

Figure 1：The Mechanism and Working Model of EF-G-catalyzed Translocation

(Source: IBP, CAS)