7QUU

Red1-Iss10 complex

7QUU の概要

• エントリーDOI: 10.2210/pdb7quu/pdb
• NMR情報: BMRB: 34702
• 分子名称: Uncharacterized protein C7D4.14c, NURS complex subunit red1 (2 entities in total)
• 機能のキーワード: mtrec complex, rna degradation, meiosis, rna
• 由来する生物種: Schizosaccharomyces pombe (fission yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 11892.48

構造登録者

Mackereth, C.D.,Kadlec, J.,Laroussi, H. (登録日: 2022-01-18, 公開日: 2022-09-07, 最終更新日: 2024-06-19)

主引用文献

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

実験手法

SOLUTION NMR