All ribosomes have a ribonucleoprotein structure made up of two unequal subunits, both of which contain three binding sites for tRNA: the A (aminoacyl), P (peptidyl) and E (exit) sites. Sequential movement of tRNAs from the A site to the P site to the E site is coupled with the movement of their associated codons in the mRNA. Translocation is induced by elongation factor G (EF-G) in bacteria, or by its eukaryotic homologue EF-2. We study how conformational changes in EF-G and the ribosome promote translocation of tRNA and mRNA.
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The central dogma of Biology is that DNA is used to make messenger RNA (mRNA), which is used to make proteins. Over the last decade, multiple findings have illuminated the importance of the regulation of protein expression at the level of mRNA translation. mRNA is no longer considered a simple courier of genetic information between DNA and protein. RNA can fold into an extensive secondary and, in many instances, tertiary structure. In recent years, numerous studies began to reveal that structured elements within the mRNA play a critical role in modulating the flow of genetic information from DNA to protein.
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