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10.1073/pnas.2017715118 http://scihub22266oqcxt.onion/10.1073/pnas.2017715118 33479166!8017934!33479166     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (6): ä Nephropedia Template TP {{tp|p=33479166|t=2021. Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome inhibits translation initiation |pdf=|usr=}}{{33479166}} gab.com Text Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome inhibits translation initiation JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=33479166 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a beta-CoV that recently emerged as a human pathogen and is the causative agent of the COVID-19 pandemic. A molecular framework of how the virus manipulates host cellular machinery to facilitate infection remains unclear. Here, we focus on SARS-CoV-2 NSP1, which is proposed to be a virulence factor that inhibits protein synthesis by directly binding the human ribosome. We demonstrate biochemically that NSP1 inhibits translation of model human and SARS-CoV-2 messenger RNAs (mRNAs). NSP1 specifically binds to the small (40S) ribosomal subunit, which is required for translation inhibition. Using single-molecule fluorescence assays to monitor NSP1-40S subunit binding in real time, we determine that eukaryotic translation initiation factors (eIFs) allosterically modulate the interaction of NSP1 with ribosomal preinitiation complexes in the absence of mRNA. We further elucidate that NSP1 competes with RNA segments downstream of the start codon to bind the 40S subunit and that the protein is unable to associate rapidly with 80S ribosomes assembled on an mRNA. Collectively, our findings support a model where NSP1 proteins from viruses in at least two subgenera of beta-CoVs associate with the open head conformation of the 40S subunit to inhibit an early step of translation, by preventing accommodation of mRNA within the entry channel. Twit Text FOAVip Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome inhibits translation initiation ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=33479166 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33479166 #FOAvip English Wikipedia <ref>{{Cite pmid|33479166}}</ref> Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome inhibits translation initiation #MMPMID33479166 Lapointe CP; Grosely R; Johnson AG; Wang J; Fernandez IS; Puglisi JD Proc Natl Acad Sci U S A 2021[Feb]; 118 (6): ä PMID33479166show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a beta-CoV that recently emerged as a human pathogen and is the causative agent of the COVID-19 pandemic. A molecular framework of how the virus manipulates host cellular machinery to facilitate infection remains unclear. Here, we focus on SARS-CoV-2 NSP1, which is proposed to be a virulence factor that inhibits protein synthesis by directly binding the human ribosome. We demonstrate biochemically that NSP1 inhibits translation of model human and SARS-CoV-2 messenger RNAs (mRNAs). NSP1 specifically binds to the small (40S) ribosomal subunit, which is required for translation inhibition. Using single-molecule fluorescence assays to monitor NSP1-40S subunit binding in real time, we determine that eukaryotic translation initiation factors (eIFs) allosterically modulate the interaction of NSP1 with ribosomal preinitiation complexes in the absence of mRNA. We further elucidate that NSP1 competes with RNA segments downstream of the start codon to bind the 40S subunit and that the protein is unable to associate rapidly with 80S ribosomes assembled on an mRNA. Collectively, our findings support a model where NSP1 proteins from viruses in at least two subgenera of beta-CoVs associate with the open head conformation of the 40S subunit to inhibit an early step of translation, by preventing accommodation of mRNA within the entry channel. |COVID-19/*genetics/*metabolism/*virology[MESH] |Eukaryotic Initiation Factors/metabolism[MESH] |Humans[MESH] |Pandemics[MESH] |Peptide Chain Initiation, Translational/genetics[MESH] |Protein Biosynthesis[MESH] |Protein Processing, Post-Translational[MESH] |RNA, Messenger/genetics/*metabolism[MESH] |RNA, Viral/genetics[MESH] |Ribosomal Proteins/genetics/metabolism[MESH] |Ribosome Subunits, Small, Eukaryotic/metabolism[MESH] |Ribosomes/genetics/*metabolism[MESH] |SARS-CoV-2/genetics/*metabolism/pathogenicity[MESH]Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribo(epmc).pdf DeepDyve Pubget Overpricing