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10.1101/gad.269068.115 http://scihub22266oqcxt.onion/10.1101/gad.269068.115 C4573856!4573856 !26294658     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26294658 &cmd=llinks): Failed to open stream: HTTP request failed! 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Mextli proteins use both canonical bipartite and novel tripartite binding modes to form eIF4E complexes that display differential sensitivity to 4E-BP regulation |pdf=|usr=}}{{26294658 }} gab.com Text Mextli proteins use both canonical bipartite and novel tripartite binding modes to form eIF4E complexes that display differential sensitivity to 4E-BP regulation JO: Genes Dev http://www.kidney.de/pget.php?&tw=1&pmid=26294658 #FOAvip The eIF4E-binding proteins (4E-BPs) are a diverse class of translation regulators that share a canonical eIF4E-binding motif (4E-BM) with eIF4G. Consequently, they compete with eIF4G for binding to eIF4E, thereby inhibiting translation initiation. Mextli (Mxt) is an unusual 4E-BP that promotes translation by also interacting with eIF3. Here we present the crystal structures of the eIF4E-binding regions of the Drosophila melanogaster (Dm) and Caenorhabditis elegans (Ce) Mxt proteins in complex with eIF4E in the cap-bound and cap-free states. The structures reveal unexpected evolutionary plasticity in the eIF4E-binding mode, with a classical bipartite interface for Ce Mxt and a novel tripartite interface for Dm Mxt. Both interfaces comprise a canonical helix and a noncanonical helix that engage the dorsal and lateral surfaces of eIF4E, respectively. Remarkably, Dm Mxt contains a C-terminal auxiliary helix that lies anti-parallel to the canonical helix on the eIF4E dorsal surface. In contrast to the eIF4G and Ce Mxt complexes, the Dm eIF4E-Mxt complexes are resistant to competition by bipartite 4E-BPs, suggesting that Dm Mxt can bind eIF4E when eIF4G binding is inhibited. Our results uncovered unexpected diversity in the binding modes of 4E-BPs, resulting in eIF4E complexes that display differential sensitivity to 4E-BP regulation. Twit Text FOAVip Mextli proteins use both canonical bipartite and novel tripartite binding modes to form eIF4E complexes that display differential sensitivity to 4E-BP regulation ????Genes Dev http://www.kidney.de/pget.php?&tw=1&pmid=26294658 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26294658 #FOAvip English Wikipedia <ref>{{Cite pmid|26294658 }}</ref> Mextli proteins use both canonical bipartite and novel tripartite binding modes to form eIF4E complexes that display differential sensitivity to 4E-BP regulation #MMPMID26294658 Peter D ; Weber R ; Köne C ; Chung MY ; Ebertsch L ; Truffault V ; Weichenrieder O ; Igreja C ; Izaurralde E Genes Dev 2015[Sep]; 29 (17 ): 1835-49 PMID26294658 show ga The eIF4E-binding proteins (4E-BPs) are a diverse class of translation regulators that share a canonical eIF4E-binding motif (4E-BM) with eIF4G. Consequently, they compete with eIF4G for binding to eIF4E, thereby inhibiting translation initiation. Mextli (Mxt) is an unusual 4E-BP that promotes translation by also interacting with eIF3. Here we present the crystal structures of the eIF4E-binding regions of the Drosophila melanogaster (Dm) and Caenorhabditis elegans (Ce) Mxt proteins in complex with eIF4E in the cap-bound and cap-free states. The structures reveal unexpected evolutionary plasticity in the eIF4E-binding mode, with a classical bipartite interface for Ce Mxt and a novel tripartite interface for Dm Mxt. Both interfaces comprise a canonical helix and a noncanonical helix that engage the dorsal and lateral surfaces of eIF4E, respectively. Remarkably, Dm Mxt contains a C-terminal auxiliary helix that lies anti-parallel to the canonical helix on the eIF4E dorsal surface. In contrast to the eIF4G and Ce Mxt complexes, the Dm eIF4E-Mxt complexes are resistant to competition by bipartite 4E-BPs, suggesting that Dm Mxt can bind eIF4E when eIF4G binding is inhibited. Our results uncovered unexpected diversity in the binding modes of 4E-BPs, resulting in eIF4E complexes that display differential sensitivity to 4E-BP regulation. |*Models, Molecular [MESH] |Animals [MESH] |Caenorhabditis elegans Proteins/*chemistry/genetics [MESH] |Caenorhabditis elegans/chemistry/genetics/metabolism [MESH] |Carrier Proteins/chemistry/genetics [MESH] |Drosophila Proteins/*chemistry/genetics [MESH] |Drosophila melanogaster/chemistry/genetics/metabolism [MESH] |Evolution, Molecular [MESH] |Gene Expression Regulation/*physiology [MESH] |Genetic Variation [MESH] |Protein Binding [MESH] |Protein Interaction Domains and Motifs/genetics/*physiology [MESH] |Protein Structure, Tertiary [MESH]Mextli proteins use both canonical bipartite and novel tripartite bind(epmc).pdf DeepDyve Pubget Overpricing