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10.7554/eLife.22883 http://scihub22266oqcxt.onion/10.7554/eLife.22883 C5336357!5336357 !28186489     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28186489 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Elife 2017 ; 6 (?): ? Nephropedia Template TP {{tp|p=28186489 |t=2017. Folding behavior of a T-shaped, ribosome-binding translation enhancer implicated in a wide-spread conformational switch |pdf=|usr=}}{{28186489 }} gab.com Text Folding behavior of a T-shaped, ribosome-binding translation enhancer implicated in a wide-spread conformational switch JO: Elife http://www.kidney.de/pget.php?&tw=1&pmid=28186489 #FOAvip Turnip crinkle virus contains a T-shaped, ribosome-binding, translation enhancer (TSS) in its 3'UTR that serves as a hub for interactions throughout the region. The viral RNA-dependent RNA polymerase (RdRp) causes the TSS/surrounding region to undergo a conformational shift postulated to inhibit translation. Using optical tweezers (OT) and steered molecular dynamic simulations (SMD), we found that the unusual stability of pseudoknotted element H4a/?(3) required five upstream adenylates, and H4a/?(3) was necessary for cooperative association of two other hairpins (H5/H4b) in Mg(2+). SMD recapitulated the TSS unfolding order in the absence of Mg(2+), showed dependence of the resistance to pulling on the 3D orientation and gave structural insights into the measured contour lengths of the TSS structure elements. Adenylate mutations eliminated one-site RdRp binding to the 3'UTR, suggesting that RdRp binding to the adenylates disrupts H4a/?(3), leading to loss of H5/H4b interaction and promoting a conformational switch interrupting translation and promoting replication. Twit Text FOAVip Folding behavior of a T-shaped, ribosome-binding translation enhancer implicated in a wide-spread conformational switch ????Elife http://www.kidney.de/pget.php?&tw=1&pmid=28186489 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28186489 #FOAvip English Wikipedia <ref>{{Cite pmid|28186489 }}</ref> Folding behavior of a T-shaped, ribosome-binding translation enhancer implicated in a wide-spread conformational switch #MMPMID28186489 Le MT ; Kasprzak WK ; Kim T ; Gao F ; Young MY ; Yuan X ; Shapiro BA ; Seog J ; Simon AE Elife 2017[Feb]; 6 (?): ? PMID28186489 show ga Turnip crinkle virus contains a T-shaped, ribosome-binding, translation enhancer (TSS) in its 3'UTR that serves as a hub for interactions throughout the region. The viral RNA-dependent RNA polymerase (RdRp) causes the TSS/surrounding region to undergo a conformational shift postulated to inhibit translation. Using optical tweezers (OT) and steered molecular dynamic simulations (SMD), we found that the unusual stability of pseudoknotted element H4a/?(3) required five upstream adenylates, and H4a/?(3) was necessary for cooperative association of two other hairpins (H5/H4b) in Mg(2+). SMD recapitulated the TSS unfolding order in the absence of Mg(2+), showed dependence of the resistance to pulling on the 3D orientation and gave structural insights into the measured contour lengths of the TSS structure elements. Adenylate mutations eliminated one-site RdRp binding to the 3'UTR, suggesting that RdRp binding to the adenylates disrupts H4a/?(3), leading to loss of H5/H4b interaction and promoting a conformational switch interrupting translation and promoting replication. |*Nucleic Acid Conformation [MESH] |*Protein Biosynthesis [MESH] |Carmovirus/*genetics [MESH] |DNA Mutational Analysis [MESH] |Molecular Dynamics Simulation [MESH] |RNA, Viral/*chemistry/*genetics [MESH] |RNA-Dependent RNA Polymerase/*metabolism [MESH]Folding behavior of a T-shaped, ribosome-binding translation enhancer (epmc).pdf DeepDyve Pubget Overpricing