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10.1016/j.bpj.2020.11.2276 http://scihub22266oqcxt.onion/10.1016/j.bpj.2020.11.2276 C7837305!7837305!33340543     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2021 ; 120 (6): 1020-30 Nephropedia Template TP {{tp|p=33340543|t=2021. Force-dependent stimulation of RNA unwinding by SARS-CoV-2 nsp13 helicase |pdf=|usr=}}{{33340543}} gab.com Text Force-dependent stimulation of RNA unwinding by SARS-CoV-2 nsp13 helicase JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=33340543 #FOAvip The superfamily 1 helicase nonstructural protein 13 (nsp13) is required for SARS-CoV-2 replication. The mechanism and regulation of nsp13 has not been explored at the single-molecule level. Specifically, force-dependent unwinding experiments have yet to be performed for any coronavirus helicase. Here, using optical tweezers, we find that nsp13 unwinding frequency, processivity, and velocity increase substantially when a destabilizing force is applied to the RNA substrate. These results, along with bulk assays, depict nsp13 as an intrinsically weak helicase that can be activated >50-fold by piconewton forces. Such force-dependent behavior contrasts the known behavior of other viral monomeric helicases, such as hepatitis C virus NS3, and instead draws stronger parallels to ring-shaped helicases. Our findings suggest that mechanoregulation, which may be provided by a directly bound RNA-dependent RNA polymerase, enables on-demand helicase activity on the relevant polynucleotide substrate during viral replication. Twit Text FOAVip Force-dependent stimulation of RNA unwinding by SARS-CoV-2 nsp13 helicase ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=33340543 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33340543 #FOAvip English Wikipedia <ref>{{Cite pmid|33340543}}</ref> Force-dependent stimulation of RNA unwinding by SARS-CoV-2 nsp13 helicase #MMPMID33340543 Mickolajczyk KJ; Shelton PM; Grasso M; Cao X; Warrington SE; Aher A; Liu S; Kapoor TM Biophys J 2021[Mar]; 120 (6): 1020-30 PMID33340543show ga The superfamily 1 helicase nonstructural protein 13 (nsp13) is required for SARS-CoV-2 replication. The mechanism and regulation of nsp13 has not been explored at the single-molecule level. Specifically, force-dependent unwinding experiments have yet to be performed for any coronavirus helicase. Here, using optical tweezers, we find that nsp13 unwinding frequency, processivity, and velocity increase substantially when a destabilizing force is applied to the RNA substrate. These results, along with bulk assays, depict nsp13 as an intrinsically weak helicase that can be activated >50-fold by piconewton forces. Such force-dependent behavior contrasts the known behavior of other viral monomeric helicases, such as hepatitis C virus NS3, and instead draws stronger parallels to ring-shaped helicases. Our findings suggest that mechanoregulation, which may be provided by a directly bound RNA-dependent RNA polymerase, enables on-demand helicase activity on the relevant polynucleotide substrate during viral replication. äForce-dependent stimulation of RNA unwinding by SARS-CoV-2 nsp13 helic(epmc).pdf DeepDyve Pubget Overpricing