7QUU

Red1-Iss10 complex

Summary for 7QUU

• Entry DOI: 10.2210/pdb7quu/pdb
• NMR Information: BMRB: 34702
• Descriptor: Uncharacterized protein C7D4.14c, NURS complex subunit red1 (2 entities in total)
• Functional Keywords: mtrec complex, rna degradation, meiosis, rna
• Biological source: Schizosaccharomyces pombe (fission yeast); More
• Total number of polymer chains: 2
• Total formula weight: 11892.48

Authors

Mackereth, C.D.,Kadlec, J.,Laroussi, H. (deposition date: 2022-01-18, release date: 2022-09-07, Last modification date: 2024-06-19)

Primary citation

Foucher, A.E.,Touat-Todeschini, L.,Juarez-Martinez, A.B.,Rakitch, A.,Laroussi, H.,Karczewski, C.,Acajjaoui, S.,Soler-Lopez, M.,Cusack, S.,Mackereth, C.D.,Verdel, A.,Kadlec, J.
Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex.
Nat Commun, 13:4969-4969, 2022

PubMed Abstract: 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.

PubMed: 36002457
DOI: 10.1038/s41467-022-32542-3

Experimental method

SOLUTION NMR