{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shuvalov A"],"funding":["Ministry of Science and Higher Education of the Russian Federation","Russian Science Foundation"],"pagination":["804-817"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8782162"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(sup2)"],"pubmed_abstract":["Nsp1 of SARS-CoV-2 regulates the translation of host and viral mRNAs in cells. Nsp1 inhibits host translation initiation by occluding the entry channel of the 40S ribosome subunit. The structural study of the Nsp1-ribosomal complexes reported post-termination 80S complex containing Nsp1, eRF1 and ABCE1. Considering the presence of Nsp1 in the post-termination 80S ribosomal complex, we hypothesized that Nsp1 may be involved in translation termination. Using a cell-free translation system and reconstituted <i>in vitro</i> 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 targe"],"journal":["RNA biology"],"pubmed_title":["Nsp1 of SARS-CoV-2 stimulates host translation termination."],"pmcid":["PMC8782162"],"funding_grant_id":["19-74-10078"],"pubmed_authors":["Matrosova V","Biziaev N","Egorova T","Arnautova A","Shuvalova E","Shuvalov A","Sokolova E","Evmenov K","Alkalaeva E","Pustogarov N"],"additional_accession":[]},"is_claimable":false,"name":"Nsp1 of SARS-CoV-2 stimulates host translation termination.","description":"Nsp1 of SARS-CoV-2 regulates the translation of host and viral mRNAs in cells. Nsp1 inhibits host translation initiation by occluding the entry channel of the 40S ribosome subunit. The structural study of the Nsp1-ribosomal complexes reported post-termination 80S complex containing Nsp1, eRF1 and ABCE1. Considering the presence of Nsp1 in the post-termination 80S ribosomal complex, we hypothesized that Nsp1 may be involved in translation termination. Using a cell-free translation system and reconstituted <i>in vitro</i> 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 targe","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Nov","modification":"2025-04-21T15:53:18.862Z","creation":"2025-04-21T15:53:18.862Z"},"accession":"S-EPMC8782162","cross_references":{"pubmed":["34793288"],"doi":["10.1080/15476286.2021.1999103"]}}