ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structure of the human MTERF4-NSUN4 protein complex that regulates mitochondrial ribosome biogenesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 138 citations in OpenAlex.
- Review
- Role of RNA 5‑methylcytosine modification in cancer: Insights from coding and non‑coding RNAs (Review).Molecular medicine reports · 2026Review
- mBiology direct · 2026Review
- NSUNs-driven dysregulation: the next frontier in targeted cancer therapy?Cell death & disease · 2025Review
- Advances in RNA modification in myocardial fibrosis (Review).International journal of molecular medicine · 2025Review
- A comprehensive tRNA pseudouridine map uncovers targets dependent on human stand-alone pseudouridine synthases.Nature cell biology · 2025Article
- Multi-omics identify ribosome related causal genes methylation, splicing, and expression in prostate cancer.Discover oncology · 2025Article
- Global Co-regulatory Cross Talk Between mMolecular neurobiology · 2025Article
- RNA 5-Methylcytosine Modification: Regulatory Molecules, Biological Functions, and Human Diseases.Genomics, proteomics & bioinformatics · 2024Review
- RNA 5-methylcytosine marks mitochondrial double-stranded RNAs for degradation and cytosolic release.Molecular cell · 2024Article
- Emerging role of RNA modification and long noncoding RNA interaction in cancer.Cancer gene therapy · 2024Review
- Review
- Molecular pathways in mitochondrial disorders due to a defective mitochondrial protein synthesis.Frontiers in cell and developmental biology · 2024Review
- RNA modification in cardiovascular disease: implications for therapeutic interventions.Signal transduction and targeted therapy · 2023Review
- RNA modification: mechanisms and therapeutic targets.Molecular biomedicine · 2023Review
- Emerging Role of RNA m5C Modification in Cardiovascular Diseases.Journal of cardiovascular translational research · 2023Review
- Deciphering the vital roles and mechanism of m5C modification on RNA in cancers.American journal of cancer research · 2023Review
- The role of m5C methyltransferases in cardiovascular diseases.Frontiers in cardiovascular medicine · 2023Review
- Pathogenic SLC25A26 variants impair SAH transport activity causing mitochondrial disease.Human molecular genetics · 2022Article
- Systematic evaluation of parameters in RNA bisulfite sequencing data generation and analysis.NAR genomics and bioinformatics · 2022Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins crucial for the respiratory chain are translated by the mitochondrial ribosome. Mitochondrial ribosome biogenesis is therefore critical for oxidative phosphorylation capacity and disturbances are known to cause human disease. This complex process is evolutionary conserved and involves several RNA processing and modification steps required for correct ribosomal RNA maturation. We recently showed that a member of the mitochondrial transcription termination factor (MTERF) family of proteins, MTERF4, recruits NSUN4, a 5-methylcytosine RNA methyltransferase, to the large ribosomal subunit in a process crucial for mitochondrial ribosome biogenesis. Here, we describe the 3D crystal structure of the human MTERF4-NSUN4 complex determined to 2.9 Å resolution. MTERF4 is composed of structurally repeated MTERF-motifs that form a nucleic acid binding domain. NSUN4 lacks an N- or C-terminal extension that is commonly used for RNA recognition by related RNA methyltransferases. Instead, NSUN4 binds to the C-terminus of MTERF4. A positively charged surface forms an RNA binding path from the concave to the convex side of MTERF4 and further along NSUN4 all of the way into the active site. This finding suggests that both subunits of the protein complex likely contribute to RNA recognition. The interface between MTERF4 and NSUN4 contains evolutionarily conserved polar and hydrophobic amino acids, and mutations that change these residues completely disrupt complex formation. This study provides a molecular explanation for MTERF4-dependent recruitment of NSUN4 to ribosomal RNA and suggests a unique mechanism by which other members of the large MTERF-family of proteins can regulate ribosomal biogenesis.
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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.