ArticleStructure (London, England : 1993)2012
Structure of the essential MTERF4:NSUN4 protein complex reveals how an MTERF protein collaborates to facilitate rRNA modification.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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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.
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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.
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Who cites it
38 citing papers in PubMed, 75 citations in OpenAlex.
- Structure-driven RNA remodeling underlies broad substrate recognition by NSUN2.Science China. Life sciences · 2026Article
- Review
- The role of mitochondrial DNA and RNA in promoting liver disease pathogenesis.Frontiers in cell and developmental biology · 2026Review
- Multi-omics identify ribosome related causal genes methylation, splicing, and expression in prostate cancer.Discover oncology · 2025Article
- The role of m5C, m1A and m7G modifications in tumors of urinary system.Frontiers in cell and developmental biology · 2025Review
- RNA 5-Methylcytosine Modification: Regulatory Molecules, Biological Functions, and Human Diseases.Genomics, proteomics & bioinformatics · 2024Review
- The role of m5C methyltransferases in cardiovascular diseases.Frontiers in cardiovascular medicine · 2023Review
- Systematic evaluation of parameters in RNA bisulfite sequencing data generation and analysis.NAR genomics and bioinformatics · 2022Article
- 5-methylcytosine RNA methyltransferases and their potential roles in cancer.Journal of translational medicine · 2022Review
- m5C RNA methyltransferase-related gene NSUN4 stimulates malignant progression of hepatocellular carcinoma and can be a prognostic marker.Cancer biomarkers : section A of Disease markers · 2022Article
- A distinct assembly pathway of the human 39S late pre-mitoribosome.Nature communications · 2021Article
- Structural basis of GTPase-mediated mitochondrial ribosome biogenesis and recycling.Nature communications · 2021Article
- Stepwise maturation of the peptidyl transferase region of human mitoribosomes.Nature communications · 2021Article
- Structural basis for late maturation steps of the human mitoribosomal large subunit.Nature communications · 2021Article
- Human Mitoribosome Biogenesis and Its Emerging Links to Disease.International journal of molecular sciences · 2021Review
- Translational adaptation to heat stress is mediated by RNA 5-methylcytosine in Caenorhabditis elegans.The EMBO journal · 2021Article
- Arabidopsis mTERF9 protein promotes chloroplast ribosomal assembly and translation by establishing ribonucleoprotein interactions in vivo.Nucleic acids research · 2021Article
- Review
- Identification, Characterization, and Expression Profile Analysis of theFrontiers in plant science · 2021Article
- Blackout in the powerhouse: clinical phenotypes associated with defects in the assembly of OXPHOS complexes and the mitoribosome.The Biochemical journal · 2020Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
MTERF4 is the first MTERF family member shown to bind RNA and plays an essential role as a regulator of ribosomal biogenesis in mammalian mitochondria. It forms a complex with the rRNA methyltransferase NSUN4 and recruits it to the large ribosomal subunit. In this article, we characterize the interaction between both proteins, demonstrate that MTERF4 strongly stimulates the specificity of NSUN4 during in vitro methylation experiments, and present the 2.0 Å resolution crystal structure of the MTERF4:NSUN4 protein complex, lacking 48 residues of the MTERF4 C-terminal acidic tail, bound to S-adenosyl-L-methionine, thus revealing the nature of the interaction between both proteins and the structural conservation of the most divergent of the human MTERF family members. Moreover, the structure suggests a model for RNA binding by the MTERF4:NSUN4 complex, providing insight into the mechanism by which an MTERF family member facilitates rRNA methylation.
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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.