ArticleNature communications2021
The zinc-finger protein Red1 orchestrates MTREC submodules and binds the Mtl1 helicase arch domain.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- Mechanisms of transcription termination across the coding and noncoding loci of the genome.Nature reviews. Molecular cell biology · 2026Review
- DNTTIP2 coordinates RNA exosome activities to ensure fidelity of human ribosome assembly.Nature communications · 2026Article
- Spliceosomal proteins direct RNA methylation to modulate gene expression and silence retrotransposons.Nature communications · 2026Article
- Direct coupling of the human nuclear exosome adaptors NEXT and PAXT with transcription termination and processing machineries.Nucleic acids research · 2026Article
- Structural basis for the synergistic assembly of the snRNA export complex.Nature structural & molecular biology · 2025Article
- A bifunctional snoRNA with separable activities in guiding rRNA 2'-O-methylation and scaffolding gametogenesis effectors.Nature communications · 2025Article
- Finding new roles of classic biomolecular condensates in the nucleus: Lessons from fission yeast.Cell insight · 2024Review
- Mapping the dynamics of epigenetic adaptation in S. pombe during heterochromatin misregulation.Developmental cell · 2024Article
- DEAD-box ATPase Dbp2 is the key enzyme in an mRNP assembly checkpoint at the 3'-end of genes and involved in the recycling of cleavage factors.Nature communications · 2024Article
- RNA quality control factors nucleate Clr4/SUV39H and trigger constitutive heterochromatin assembly.Cell · 2024Article
- Dual agonistic and antagonistic roles of ZC3H18 provide for co-activation of distinct nuclear RNA decay pathways.Cell reports · 2023Article
- PAPγ associates with PAXT nuclear exosome to control the abundance of PROMPT ncRNAs.Nature communications · 2023Article
- The molecular basis of heterochromatin assembly and epigenetic inheritance.Molecular cell · 2023Review
- Mechanistic insights into RNA surveillance by the canonical poly(A) polymerase Pla1 of the MTREC complex.Nature communications · 2023Article
- Extended N-Terminal Acetyltransferase Naa50 in Filamentous Fungi Adds to Naa50 Diversity.International journal of molecular sciences · 2022Article
- The inner nuclear membrane protein Lem2 coordinates RNA degradation at the nuclear periphery.Nature structural & molecular biology · 2022Article
- Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex.Nature communications · 2022Article
- The human SKI complex regulates channeling of ribosome-bound RNA to the exosome via an intrinsic gatekeeping mechanism.Molecular cell · 2022Article
- RNA binding proteins in osteoarthritis.Frontiers in cell and developmental biology · 2022Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cryptic unstable transcripts (CUTs) are rapidly degraded by the nuclear exosome in a process requiring the RNA helicase Mtr4 and specific adaptor complexes for RNA substrate recognition. The PAXT and MTREC complexes have recently been identified as homologous exosome adaptors in human and fission yeast, respectively. The eleven-subunit MTREC comprises the zinc-finger protein Red1 and the Mtr4 homologue Mtl1. Here, we use yeast two-hybrid and pull-down assays to derive a detailed interaction map. We show that Red1 bridges MTREC submodules and serves as the central scaffold. In the crystal structure of a minimal Mtl1/Red1 complex an unstructured region adjacent to the Red1 zinc-finger domain binds to both the Mtl1 KOW domain and stalk helices. This interaction extends the canonical interface seen in Mtr4-adaptor complexes. In vivo mutational analysis shows that this interface is essential for cell survival. Our results add to Mtr4 versatility and provide mechanistic insights into the MTREC complex.
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