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10.1083/jcb.201502103 http://scihub22266oqcxt.onion/10.1083/jcb.201502103 C4602035!4602035 !26459600     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26459600 &cmd=llinks): Failed to open stream: HTTP request failed! 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Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon |pdf=|usr=}}{{26459600 }} gab.com Text Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon JO: J Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=26459600 #FOAvip Cotranslational protein targeting delivers proteins to the bacterial cytoplasmic membrane or to the eukaryotic endoplasmic reticulum membrane. The signal recognition particle (SRP) binds to signal sequences emerging from the ribosomal tunnel and targets the ribosome-nascent-chain complex (RNC) to the SRP receptor, termed FtsY in bacteria. FtsY interacts with the fifth cytosolic loop of SecY in the SecYEG translocon, but the functional role of the interaction is unclear. By using photo-cross-linking and fluorescence resonance energy transfer measurements, we show that FtsY-SecY complex formation is guanosine triphosphate independent but requires a phospholipid environment. Binding of an SRP-RNC complex exposing a hydrophobic transmembrane segment induces a rearrangement of the SecY-FtsY complex, which allows the subsequent contact between SecY and ribosomal protein uL23. These results suggest that direct RNC transfer to the translocon is guided by the interaction between SRP and translocon-bound FtsY in a quaternary targeting complex. Twit Text FOAVip Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon ????J Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=26459600 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26459600 #FOAvip English Wikipedia <ref>{{Cite pmid|26459600 }}</ref> Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon #MMPMID26459600 Kuhn P ; Draycheva A ; Vogt A ; Petriman NA ; Sturm L ; Drepper F ; Warscheid B ; Wintermeyer W ; Koch HG J Cell Biol 2015[Oct]; 211 (1 ): 91-104 PMID26459600 show ga Cotranslational protein targeting delivers proteins to the bacterial cytoplasmic membrane or to the eukaryotic endoplasmic reticulum membrane. The signal recognition particle (SRP) binds to signal sequences emerging from the ribosomal tunnel and targets the ribosome-nascent-chain complex (RNC) to the SRP receptor, termed FtsY in bacteria. FtsY interacts with the fifth cytosolic loop of SecY in the SecYEG translocon, but the functional role of the interaction is unclear. By using photo-cross-linking and fluorescence resonance energy transfer measurements, we show that FtsY-SecY complex formation is guanosine triphosphate independent but requires a phospholipid environment. Binding of an SRP-RNC complex exposing a hydrophobic transmembrane segment induces a rearrangement of the SecY-FtsY complex, which allows the subsequent contact between SecY and ribosomal protein uL23. These results suggest that direct RNC transfer to the translocon is guided by the interaction between SRP and translocon-bound FtsY in a quaternary targeting complex. |*Protein Biosynthesis [MESH] |Adenosine Triphosphatases/chemistry [MESH] |Bacterial Proteins/chemistry [MESH] |Binding, Competitive [MESH] |Escherichia coli [MESH] |Escherichia coli Proteins/*chemistry [MESH] |Lipids/chemistry [MESH] |Membrane Transport Proteins/chemistry [MESH] |Protein Binding [MESH] |Receptors, Cytoplasmic and Nuclear/chemistry [MESH] |Receptors, Peptide [MESH] |Ribosomes/chemistry [MESH] |SEC Translocation Channels [MESH] |SecA Proteins [MESH]Ribosome binding induces repositioning of the signal recognition parti(epmc).pdf DeepDyve Pubget Overpricing