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10.1093/nar/gkv856 http://scihub22266oqcxt.onion/10.1093/nar/gkv856 C4627077!4627077 !26338772     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26338772 &cmd=llinks): Failed to open stream: HTTP request failed! 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EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP exits the ribosome via two different pathways |pdf=|usr=}}{{26338772 }} gab.com Text EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP exits the ribosome via two different pathways JO: Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=26338772 #FOAvip The G-protein EF-Tu, which undergoes a major conformational change when EF-Tu·GTP is converted to EF-Tu·GDP, forms part of an aminoacyl(aa)-tRNA·EF-Tu·GTP ternary complex (TC) that accelerates the binding of aa-tRNA to the ribosome during peptide elongation. Such binding, placing a portion of EF-Tu in contact with the GTPase Associated Center (GAC), is followed by GTP hydrolysis and Pi release, and results in formation of a pretranslocation (PRE) complex. Although tRNA movement through the ribosome during PRE complex formation has been extensively studied, comparatively little is known about the dynamics of EF-Tu interaction with either the ribosome or aa-tRNA. Here we examine these dynamics, utilizing ensemble and single molecule assays employing fluorescent labeled derivatives of EF-Tu, tRNA, and the ribosome to measure changes in either FRET efficiency or fluorescence intensity during PRE complex formation. Our results indicate that ribosome-bound EF-Tu separates from the GAC prior to its full separation from aa-tRNA, and suggest that EF-Tu·GDP dissociates from the ribosome by two different pathways. These pathways correspond to either reversible EF-Tu·GDP dissociation from the ribosome prior to the major conformational change in EF-Tu that follows GTP hydrolysis, or irreversible dissociation after or concomitant with this conformational change. Twit Text FOAVip EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP exits the ribosome via two different pathways ????Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=26338772 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26338772 #FOAvip English Wikipedia <ref>{{Cite pmid|26338772 }}</ref> EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP exits the ribosome via two different pathways #MMPMID26338772 Liu W ; Chen C ; Kavaliauskas D ; Knudsen CR ; Goldman YE ; Cooperman BS Nucleic Acids Res 2015[Oct]; 43 (19 ): 9519-28 PMID26338772 show ga The G-protein EF-Tu, which undergoes a major conformational change when EF-Tu·GTP is converted to EF-Tu·GDP, forms part of an aminoacyl(aa)-tRNA·EF-Tu·GTP ternary complex (TC) that accelerates the binding of aa-tRNA to the ribosome during peptide elongation. Such binding, placing a portion of EF-Tu in contact with the GTPase Associated Center (GAC), is followed by GTP hydrolysis and Pi release, and results in formation of a pretranslocation (PRE) complex. Although tRNA movement through the ribosome during PRE complex formation has been extensively studied, comparatively little is known about the dynamics of EF-Tu interaction with either the ribosome or aa-tRNA. Here we examine these dynamics, utilizing ensemble and single molecule assays employing fluorescent labeled derivatives of EF-Tu, tRNA, and the ribosome to measure changes in either FRET efficiency or fluorescence intensity during PRE complex formation. Our results indicate that ribosome-bound EF-Tu separates from the GAC prior to its full separation from aa-tRNA, and suggest that EF-Tu·GDP dissociates from the ribosome by two different pathways. These pathways correspond to either reversible EF-Tu·GDP dissociation from the ribosome prior to the major conformational change in EF-Tu that follows GTP hydrolysis, or irreversible dissociation after or concomitant with this conformational change. |*Peptide Chain Elongation, Translational [MESH] |Fluorescence Resonance Energy Transfer [MESH] |Guanosine Diphosphate/*metabolism [MESH] |Guanosine Triphosphate/metabolism [MESH] |Peptide Elongation Factor Tu/*metabolism [MESH] |RNA, Transfer, Amino Acyl/metabolism [MESH] |Ribosomal Proteins/metabolism [MESH]EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP e(epmc).pdf DeepDyve Pubget Overpricing