Structural assembly of the nucleic-acid-binding Thp3–Csn12–Sem1 complex functioning in mRNA splicing

التفاصيل البيبلوغرافية
العنوان: Structural assembly of the nucleic-acid-binding Thp3–Csn12–Sem1 complex functioning in mRNA splicing
المؤلفون: Zhiling Kuang, Jiyuan Ke, Jiong Hong, Zhongliang Zhu, Liwen Niu
المصدر: Nucleic Acids Research. 50:8882-8897
بيانات النشر: Oxford University Press (OUP), 2022.
سنة النشر: 2022
مصطلحات موضوعية: Percutaneous Coronary Intervention, Saccharomyces cerevisiae Proteins, RNA Splicing, RNA Precursors, Genetics, RNA, Messenger, Saccharomyces cerevisiae
الوصف: PCI domain proteins play important roles in post-transcriptional gene regulation. In the TREX-2 complex, PCI domain-containing Sac3 and Thp1 proteins and accessory Sem1 protein form a ternary complex required for mRNA nuclear export. In contrast, structurally related Thp3–Csn12–Sem1 complex mediates pre-mRNA splicing. In this study, we determined the structure of yeast Thp3186–470–Csn12–Sem1 ternary complex at 2.9 Å resolution. Both Thp3 and Csn12 structures have a typical PCI structural fold, characterized by a stack of α-helices capped by a C-terminal winged-helix (WH) domain. The overall structure of Thp3186–470–Csn12–Sem1 complex has an inverted V-shape with Thp3 and Csn12 forming the two sides. A fishhook-shaped Sem1 makes extensive contacts on Csn12 to stabilize its conformation. The overall structure of Thp3186–470–Csn12–Sem1 complex resembles the previously reported Sac3–Thp1–Sem1 complex, but also has significant structural differences. The C-terminal WH domains of Thp3 and Csn12 form a continuous surface to bind different forms of nucleic acids with micromolar affinity. Mutation of the basic residues in the WH domains of Thp3 and Csn12 affects nucleic acid binding in vitro and mRNA splicing in vivo. The Thp3–Csn12–Sem1 structure provides a foundation for further exploring the structural elements required for its specific recruitment to spliceosome for pre-mRNA splicing.
تدمد: 1362-4962
0305-1048
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74ca3ea87e59a9d7e02c491d9a543402
https://doi.org/10.1093/nar/gkac634
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....74ca3ea87e59a9d7e02c491d9a543402
قاعدة البيانات: OpenAIRE