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10.1016/j.pep.2021.105894 http://scihub22266oqcxt.onion/10.1016/j.pep.2021.105894 33933612!8082334!33933612     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       Protein+Expr+Purif 2021 ; 185 (ä): 105894 Nephropedia Template TP {{tp|p=33933612|t=2021. Reconstitution and functional characterization of SARS-CoV-2 proofreading complex |pdf=|usr=}}{{33933612}} gab.com Text Reconstitution and functional characterization of SARS-CoV-2 proofreading complex JO: Protein Expr Purif http://www.kidney.de/pget.php?&tw=1&pmid=33933612 #FOAvip The novel Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2 or COVID-19) has led to a world-wild pandemic. The replication of SARS-CoV-2 RNA genome involves the core replication-transcription complex (RTC, nsp12-nsp7-nsp8) and the proofreading complex (nsp14-nsp10) that can correct mismatched base pairs during replication. Structures and functions of SARS-CoV-2 RTC have been actively studied, yet little is known about SARS-CoV-2 nsp14-nsp10. Here, we purified, reconstituted, and characterized the SARS-CoV-2 nsp14-nsp10 proofreading nuclease in vitro. We show that SARS-CoV-2 nsp14 is activated by nsp10, functioning as a potent RNase that can hydrolyze RNAs in the context of single- and double-stranded RNA and RNA/DNA hybrid duplex. SARS-CoV-2 nsp14-nsp10 shows a metal-dependent nuclease activity but has different metal selectivity from RTC. While RTC is activated by Ca(2+), nsp14-nsp10 is completely inhibited. Importantly, the reconstituted SARS-CoV-2 nsp14-nsp10 efficiently removed the A:A mismatch at the 3'-end of the primer, enabling the stalled RTC to restart RNA replication. Our collective results confirm that SARS-CoV-2 nsp14-nsp10 functions as the RNA proofreading complex in SARS-CoV-2 replication and provide a useful foundation to understand the structure and function of SARS-CoV-2 RNA metabolism. Twit Text FOAVip Reconstitution and functional characterization of SARS-CoV-2 proofreading complex ????Protein Expr Purif http://www.kidney.de/pget.php?&tw=1&pmid=33933612 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33933612 #FOAvip English Wikipedia <ref>{{Cite pmid|33933612}}</ref> Reconstitution and functional characterization of SARS-CoV-2 proofreading complex #MMPMID33933612 Ma Z; Pourfarjam Y; Kim IK Protein Expr Purif 2021[Sep]; 185 (ä): 105894 PMID33933612show ga The novel Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2 or COVID-19) has led to a world-wild pandemic. The replication of SARS-CoV-2 RNA genome involves the core replication-transcription complex (RTC, nsp12-nsp7-nsp8) and the proofreading complex (nsp14-nsp10) that can correct mismatched base pairs during replication. Structures and functions of SARS-CoV-2 RTC have been actively studied, yet little is known about SARS-CoV-2 nsp14-nsp10. Here, we purified, reconstituted, and characterized the SARS-CoV-2 nsp14-nsp10 proofreading nuclease in vitro. We show that SARS-CoV-2 nsp14 is activated by nsp10, functioning as a potent RNase that can hydrolyze RNAs in the context of single- and double-stranded RNA and RNA/DNA hybrid duplex. SARS-CoV-2 nsp14-nsp10 shows a metal-dependent nuclease activity but has different metal selectivity from RTC. While RTC is activated by Ca(2+), nsp14-nsp10 is completely inhibited. Importantly, the reconstituted SARS-CoV-2 nsp14-nsp10 efficiently removed the A:A mismatch at the 3'-end of the primer, enabling the stalled RTC to restart RNA replication. Our collective results confirm that SARS-CoV-2 nsp14-nsp10 functions as the RNA proofreading complex in SARS-CoV-2 replication and provide a useful foundation to understand the structure and function of SARS-CoV-2 RNA metabolism. |COVID-19/*virology[MESH] |Calcium/metabolism[MESH] |Enzyme Activation[MESH] |Exoribonucleases/*metabolism[MESH] |Humans[MESH] |Hydrolysis[MESH] |RNA, Viral/*metabolism[MESH] |SARS-CoV-2/*metabolism[MESH] |Substrate Specificity[MESH] |Viral Nonstructural Proteins/*metabolism[MESH]Reconstitution and functional characterization of SARS-CoV-2 proofread(epmc).pdf DeepDyve Pubget Overpricing