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10.1093/nar/gkv809 http://scihub22266oqcxt.onion/10.1093/nar/gkv809 C4605303!4605303 !26275778     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26275778 &cmd=llinks): Failed to open stream: HTTP request failed! 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NUFIP and the HSP90/R2TP chaperone bind the SMN complex and facilitate assembly of U4-specific proteins |pdf=|usr=}}{{26275778 }} gab.com Text NUFIP and the HSP90/R2TP chaperone bind the SMN complex and facilitate assembly of U4-specific proteins JO: Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=26275778 #FOAvip The Sm proteins are loaded on snRNAs by the SMN complex, but how snRNP-specific proteins are assembled remains poorly characterized. U4 snRNP and box C/D snoRNPs have structural similarities. They both contain the 15.5K and proteins with NOP domains (PRP31 for U4, NOP56/58 for snoRNPs). Biogenesis of box C/D snoRNPs involves NUFIP and the HSP90/R2TP chaperone system and here, we explore the function of this machinery in U4 RNP assembly. We show that yeast Prp31 interacts with several components of the NUFIP/R2TP machinery, and that these interactions are separable from each other. In human cells, PRP31 mutants that fail to stably associate with U4 snRNA still interact with components of the NUFIP/R2TP system, indicating that these interactions precede binding of PRP31 to U4 snRNA. Knock-down of NUFIP leads to mislocalization of PRP31 and decreased association with U4. Moreover, NUFIP is associated with the SMN complex through direct interactions with Gemin3 and Gemin6. Altogether, our data suggest a model in which the NUFIP/R2TP system is connected with the SMN complex and facilitates assembly of U4 snRNP-specific proteins. Twit Text FOAVip NUFIP and the HSP90/R2TP chaperone bind the SMN complex and facilitate assembly of U4-specific proteins ????Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=26275778 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26275778 #FOAvip English Wikipedia <ref>{{Cite pmid|26275778 }}</ref> NUFIP and the HSP90/R2TP chaperone bind the SMN complex and facilitate assembly of U4-specific proteins #MMPMID26275778 Bizarro J ; Dodré M ; Huttin A ; Charpentier B ; Schlotter F ; Branlant C ; Verheggen C ; Massenet S ; Bertrand E Nucleic Acids Res 2015[Oct]; 43 (18 ): 8973-89 PMID26275778 show ga The Sm proteins are loaded on snRNAs by the SMN complex, but how snRNP-specific proteins are assembled remains poorly characterized. U4 snRNP and box C/D snoRNPs have structural similarities. They both contain the 15.5K and proteins with NOP domains (PRP31 for U4, NOP56/58 for snoRNPs). Biogenesis of box C/D snoRNPs involves NUFIP and the HSP90/R2TP chaperone system and here, we explore the function of this machinery in U4 RNP assembly. We show that yeast Prp31 interacts with several components of the NUFIP/R2TP machinery, and that these interactions are separable from each other. In human cells, PRP31 mutants that fail to stably associate with U4 snRNA still interact with components of the NUFIP/R2TP system, indicating that these interactions precede binding of PRP31 to U4 snRNA. Knock-down of NUFIP leads to mislocalization of PRP31 and decreased association with U4. Moreover, NUFIP is associated with the SMN complex through direct interactions with Gemin3 and Gemin6. Altogether, our data suggest a model in which the NUFIP/R2TP system is connected with the SMN complex and facilitates assembly of U4 snRNP-specific proteins. |Cell Line [MESH] |Coiled Bodies/metabolism [MESH] |Cytoplasm/metabolism [MESH] |Eye Proteins/chemistry/genetics/*metabolism [MESH] |HeLa Cells [MESH] |Humans [MESH] |Molecular Chaperones/*metabolism [MESH] |Mutagenesis, Insertional [MESH] |RNA, Small Nuclear/metabolism [MESH] |Ribonucleoprotein, U4-U6 Small Nuclear/*metabolism [MESH] |Ribonucleoproteins, Small Nuclear/metabolism [MESH] |Ribonucleoproteins, Small Nucleolar/metabolism [MESH] |Ribosomal Proteins/*metabolism [MESH] |SMN Complex Proteins/*metabolism [MESH] |Saccharomyces cerevisiae Proteins/genetics/*metabolism [MESH]NUFIP and the HSP90/R2TP chaperone bind the SMN complex and facilitate(epmc).pdf DeepDyve Pubget Overpricing