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Nsp1 of SARS-CoV-2 stimulates host translation termination

Alexey Shuvalov, Ekaterina Shuvalova, Nikita Biziaev, Elizaveta Sokolova, Konstantin Evmenov, Nikolay Pustogarov, Aleksandra Arnautova, Vera A. Matrosova, Tatiana Egorova, Elena Alkalaeva

2021RNA Biology21 citationsDOIOpen Access PDF

Abstract

translation system, we show that Nsp1 stimulates peptide release and formation of termination complexes. Detailed analysis of Nsp1 activity during translation termination stages reveals that Nsp1 facilitates stop codon recognition. We demonstrate that Nsp1 stimulation targets eRF1 and does not affect eRF3. Moreover, Nsp1 increases amount of the termination complexes at all three stop codons. The activity of Nsp1 in translation termination is provided by its N-terminal domain and the minimal required part of eRF1 is NM domain. We assume that the biological meaning of Nsp1 activity in translation termination is binding with the 80S ribosomes translating host mRNAs and remove them from the pool of the active ribosomes.

Topics & Concepts

RibosomeTranslation (biology)BiologyCell biologyStop codonRibosomal RNATranslational frameshiftProtein biosynthesisEukaryotic RibosomeMessenger RNARNAGeneticsGeneRNA and protein synthesis mechanismsViral Infections and Immunology ResearchRNA Interference and Gene Delivery
Nsp1 of SARS-CoV-2 stimulates host translation termination | Litcius