ArticleNature communications2026
Structural basis of TACO1-mediated efficient mitochondrial translation.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026Review
- eIF5A and polyamines restrict mRNA levels in response to ribosome stalls.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Enhancing ribosomal translation of backbone-altering nonproteinogenic amino acids via YebC and YeeN.Nucleic acids research · 2026Article
- Copper transport to mitochondria by SLC25A3 contributes to skeletal myoblast differentiation and is required for survival of differentiated myotubes.bioRxiv : the preprint server for biology · 2026Article
- Structure determination and dual targeting of a plant TACO1 identifies its ancient role as an organelle translation regulator.bioRxiv : the preprint server for biology · 2026Article
- TACO1 regulates mitochondrial adaptation in hypertension-induced cardiac remodeling and heart failure.Research square · 2026Article
- When membrane insertion sets the pace of mitochondrial translation.Nature structural & molecular biology · 2026Article
- Membrane insertion of mitochondrial-encoded proteins regulates ribosome decoding speed.Nature structural & molecular biology · 2026Article
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7 authors.
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Abstract
Translation elongation is a universally conserved step in protein synthesis, relying on elongation factors that engage the ribosomal L7/L12 stalk to mediate aminoacyl-tRNA delivery, accommodation, and ribosomal translocation. Using in organello cryo-electron microscopy, we reveal how the mitochondrial translation accelerator TACO1 promotes efficient elongation on human mitoribosomes. TACO1 binds the mitoribosomal region typically bound by elongation factor Tu (mtEF-Tu), bridging the large and small subunits via contacts with 16S rRNA, bL12m, A-site tRNA, and uS12m. While active throughout elongation, TACO1 is especially critical when translating polyproline motifs. Its absence prolongs mtEF-Tu residence in A/T states, causes persistent mitoribosomal stalling and premature subunit dissociation. Structural analyses indicate that TACO1 competes with mtEF-Tu for mitoribosome binding, stabilizes A-site tRNA, and enhances peptidyl transfer through a mechanism distinct from EF-P and eIF5A. These findings suggest that bacterial TACO1 orthologs may serve analogous roles, highlighting an evolutionarily conserved strategy for maintaining elongation efficiency during challenging translation events.
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