{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["42(3)"],"submitter":["Rothe B"],"pubmed_abstract":["The yeast Snu13p protein and its 15.5K human homolog both bind U4 snRNA and box C/D snoRNAs. They also bind the Rsa1p/NUFIP assembly factor, proposed to scaffold immature snoRNPs and to recruit the Hsp90-R2TP chaperone complex. However, the nature of the Snu13p/15.5K-Rsa1p/NUFIP interaction and its exact role in snoRNP assembly remained to be elucidated. By using biophysical, molecular and imaging approaches, here, we identify residues needed for Snu13p/15.5K-Rsa1p/NUFIP interaction. By NMR structure determination and docking approaches, we built a 3D model of the Snup13p-Rsa1p interface, suggesting that residues R249, R246 and K250 in Rsa1p and E72 and D73 in Snu13p form a network of electrostatic interactions shielded from the solvent by hydrophobic residues from both proteins and that r"],"journal":["Nucleic acids research"],"pagination":["2015-36"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3919607"],"repository":["biostudies-literature"],"pubmed_title":["Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly."],"pmcid":["PMC3919607"],"pubmed_authors":["Bizarro J","Robert MC","Romier C","Quinternet M","Manival X","Bertrand E","Branlant C","Blaud M","Charpentier B","Rothe B","Back R"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly.","description":"The yeast Snu13p protein and its 15.5K human homolog both bind U4 snRNA and box C/D snoRNAs. They also bind the Rsa1p/NUFIP assembly factor, proposed to scaffold immature snoRNPs and to recruit the Hsp90-R2TP chaperone complex. However, the nature of the Snu13p/15.5K-Rsa1p/NUFIP interaction and its exact role in snoRNP assembly remained to be elucidated. By using biophysical, molecular and imaging approaches, here, we identify residues needed for Snu13p/15.5K-Rsa1p/NUFIP interaction. By NMR structure determination and docking approaches, we built a 3D model of the Snup13p-Rsa1p interface, suggesting that residues R249, R246 and K250 in Rsa1p and E72 and D73 in Snu13p form a network of electrostatic interactions shielded from the solvent by hydrophobic residues from both proteins and that r","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Feb","modification":"2026-04-29T22:43:26.755Z","creation":"2019-03-27T01:21:34Z"},"accession":"S-EPMC3919607","cross_references":{"pubmed":["24234454"],"doi":["10.1093/nar/gkt1091"]}}