Abstract
This paper is a review of currently available data concerning interactions of tRNAs with the eukaryotic ribosome at various stages of translation. These data include the results obtained by means of cryo-electron microscopy and X-ray crystallography applied to various model ribosomal complexes, site-directed cross-linking with the use of tRNA derivatives bearing chemically or photochemically reactive groups in the CCA-terminal fragment and chemical probing of 28S rRNA in the region of the peptidyl transferase center. Similarities and differences in the interactions of tRNAs with prokaryotic and eukaryotic ribosomes are discussed with concomitant consideration of the extent of resemblance between molecular mechanisms of translation in eukaryotes and bacteria.
Highlights
Amino acid residues necessary for protein synthesis are delivered to ribosomes by tRNA molecules with the aid of special translation factors
Correspondence of mRNA codons and amino acid residues is determined by the genetic code, which is almost universal in all domains of life
This review summarizes recently obtained data on interaction of tRNA with translation factors and the cytoplasmic eukaryotic ribosome in classical and hybrid states during initiation and elongation steps
Summary
Amino acid residues necessary for protein synthesis are delivered to ribosomes by tRNA molecules with the aid of special translation factors. It has been found out that (i) binding of tRNAs to the ribosomal P site depends strongly, and to the A site completely, on the presence of cognate codon and can be observed with either charged or deacylated tRNAs; (ii) binding at the A and P sites is determined mainly by the small ribosomal subunit, which can bind tRNAs independently of the large subunit; (iii) E site binding can take place only with deacylated tRNA, it depends weakly (or does not depend at all) on the nature of codon placed at the E site and occurs mainly at the large subunit; (iv) tRNAs in all forms have higher affinity to the P site than to the A or the E sites These binding properties were widely used to obtain various model complexes of ribosomes with tRNAs for studying positioning of mRNA codons and of tRNA in the ribosome by means of site-directed cross-linking (e.g., [22,23,24,25,33,34]), cryo-EM (e.g., [14,18]) and X-ray crystallography (e.g., [35,36,37,38]) and by other methods, e.g., single-molecule fluorescence resonance energy transfer (FRET) [14,39,40,41].
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