7quu

Red1-Iss10 complexRed1-Iss10 complex

Structural highlights 7quu is a 2 chain structure with sequence from Schizosaccharomyces pombe. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function YFPE_SCHPO Publication Abstract from PubMed To eliminate specific or aberrant transcripts, eukaryotes use nuclear RNA-targeting complexes that deliver them to the exosome for degradation. S. pombe MTREC, and its human counterpart PAXT, are key players in this mechanism but inner workings of these complexes are not understood in sufficient detail. Here, we present an NMR structure of an MTREC scaffold protein Red1 helix-turn-helix domain bound to the Iss10 N-terminus and show this interaction is required for proper cellular growth and meiotic mRNA degradation. We also report a crystal structure of a Red1-Ars2 complex explaining mutually exclusive interactions of hARS2 with various ED/EGEI/L motif-possessing RNA regulators, including hZFC3H1 of PAXT, hFLASH or hNCBP3. Finally, we show that both Red1 and hZFC3H1 homo-dimerize via their coiled-coil regions indicating that MTREC and PAXT likely function as dimers. Our results, combining structures of three Red1 interfaces with in vivo studies, provide mechanistic insights into conserved features of MTREC/PAXT architecture. Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex.,Foucher AE, Touat-Todeschini L, Juarez-Martinez AB, Rakitch A, Laroussi H, Karczewski C, Acajjaoui S, Soler-Lopez M, Cusack S, Mackereth CD, Verdel A, Kadlec J Nat Commun. 2022 Aug 24;13(1):4969. doi: 10.1038/s41467-022-32542-3. PMID:36002457 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 7quu Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image