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Enter brief annotation of your abstract in this text form (around 250 words)

Ribosome is a giant ribonucleoprotein machinery, which synthesizes proteins in all organisms from bacteria to human according to the program incoming as messenger RNA (mRNA) copied from definite parts of the genomic DNA. Structures of ribosomes from all kingdoms of life to date are deciphered at near-atomic level thanks to achievements in X-ray crystallography and cryo-electron microscopy. Thus, specific amino acid residues of ribosomal proteins (RPs) contacting mRNAs and tRNAs are known. However, structural information itself does not provide an idea on contributions of these contacts to the translation process and its regulation and it remained unclear which consequences would take place upon changes at amino acid residues contacting mRNAs and tRNAs. This information has been obtained recently in our studies. With the use of human cells producing labeled target ribosomal protein with an alteration at amino acids residues under investigation, we identified functional assignment of the C-terminal tail of RP uS19, and conserved motifs 60-GEKG-63 of RP uS3, YxxPKxYxK of the RP eS26 and 45-QSGYGGQTK-53 of the RP eL42 (L36AL). 

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