REVIEW: The NeverEnding E-Story

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Valeriy G. Metelev¹ and Alexey A. Bogdanov^1,2,3,a*

¹Faculty of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia

²Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russia

³Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, 117997 Moscow, Russia

^* To whom correspondence should be addressed.

Received: August 11, 2025; Revised: September 16, 2025; Accepted: September 17, 2025

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The review discusses the functional role of the ribosomal E-site in the context of recent structural data. Traditionally, the E-site has been considered to serve only as a binding site for deacylated tRNA (E-tRNA) prior to its dissociation from the protein synthesis complex. Here, we examine specific contacts formed between E-tRNA and rRNA of the large ribosomal subunit in different organisms, as well as the sequence of their formation and disruption. The mechanism of translation suppression by inhibitors that bind to the ribosomal E-site is discussed. Based on current evidence regarding the location of aminoacyl-tRNA synthetases (ARSs) in the immediate vicinity of the ribosome, we propose a hypothesis that one of the primary functions of the ribosomal E-site is to prepare tRNA (through its modulation) for the formation of a specific complex with ARS, in the content of which it is released from the ribosome.

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KEY WORDS: E-site of the ribosome, E-tRNA, translation inhibitors, aminoacyl-tRNA synthetases

DOI: 10.1134/S0006297925602503

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