ArticleNucleic acids research2016
A novel RNA-binding mode of the YTH domain reveals the mechanism for recognition of determinant of selective removal by Mmi1.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
50 citing papers in PubMed.
- The Nucleic Acids' Immunoprecipitation Method for DNA Repair Research.Methods in molecular biology (Clifton, N.J.) · 2026Article
- RNA-Binding Proteins in Dinoflagellates.International journal of molecular sciences · 2026Review
- Genome-Wide Identification and Evolutionary Analysis of m6A-Related Gene Family in Poplar Nanlin895.Plants (Basel, Switzerland) · 2025Article
- A bifunctional snoRNA with separable activities in guiding rRNA 2'-O-methylation and scaffolding gametogenesis effectors.Nature communications · 2025Article
- Article
- ALBA proteins facilitate cytoplasmic YTHDF-mediated reading of m6A in Arabidopsis.The EMBO journal · 2024Article
- Reading mJournal of integrative plant biology · 2024Review
- RNA quality control factors nucleate Clr4/SUV39H and trigger constitutive heterochromatin assembly.Cell · 2024Article
- mRNA nuclear export: how mRNA identity features distinguish functional RNAs from junk transcripts.RNA biology · 2024Review
- Current progress in strategies to profile transcriptomic mFrontiers in cell and developmental biology · 2024Review
- Emerging roles of RNA binding proteins in intervertebral disc degeneration and osteoarthritis.Orthopaedic surgery · 2023Review
- Insights into the conservation and diversification of the molecular functions of YTHDF proteins.PLoS genetics · 2023Article
- The Proteins of mRNA Modification: Writers, Readers, and Erasers.Annual review of biochemistry · 2023Review
- Epitranscriptomics in parasitic protists: Role of RNA chemical modifications in posttranscriptional gene regulation.PLoS pathogens · 2022Review
- Article
- Structural insights reveal the specific recognition of meiRNA by the Mei2 protein.Journal of molecular cell biology · 2022Article
- YTH Domain Proteins Play an Essential Role in Rice Growth and Stress Response.Plants (Basel, Switzerland) · 2022Article
- Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex.Nature communications · 2022Article
- YTHDC2 control of gametogenesis requires helicase activity but not mGenes & development · 2022Article
- Long RNA-Mediated Chromatin Regulation in Fission Yeast and Mammals.International journal of molecular sciences · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The YTH domain-containing protein Mmi1, together with other factors, constitutes the machinery used to selectively remove meiosis-specific mRNA during the vegetative growth of fission yeast. Mmi1 directs meiotic mRNAs to the nuclear exosome for degradation by recognizing their DSR (determinant of selective removal) motif. Here, we present the crystal structure of the Mmi1 YTH domain in the apo state and in complex with a DSR motif, demonstrating that the Mmi1 YTH domain selectively recognizes the DSR motif. Intriguingly, Mmi1 also contains a potential m(6)A (N(6)-methyladenine)-binding pocket, but its binding of the DSR motif is dependent on a long groove opposite the m(6)A pocket. The DSR-binding mode is distinct from the m(6)A RNA-binding mode utilized by other YTH domains. Furthermore, the m(6)A pocket cannot bind m(6)A RNA. Our structural and biochemical experiments uncover the mechanism of the YTH domain in binding the DSR motif and help to elucidate the function of Mmi1.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.