ArticleGenes & development2006
A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae.
Article in Genes & development, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 165 citations in OpenAlex.
- Heterodera schachtii enolase does not elicit canonical immune responses in Arabidopsis thaliana.Scientific reports · 2026Article
- Towards CRISPR-based editing of the mitochondrial genome in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Surface enolase is a virulence factor ofFrontiers in microbiology · 2026Article
- Hexokinase 2 is an RNA-binding protein that regulates mRNA translation independently of glycolysis and induces melanoma cell proliferation.PLoS biology · 2025Article
- Moonlighting Proteins: Unveiling Their Multifunctionality in Metabolic Regulation and Drug Discovery.Current drug metabolism · 2025Review
- Circular RNA circESYT2 serves as a microRNA-665 sponge to promote the progression of hepatocellular carcinoma through ENO2.Cancer science · 2024Article
- Multifunctional roles of γ-enolase in the central nervous system: more than a neuronal marker.Cell & bioscience · 2024Review
- Two ancient membrane pores mediate mitochondrial-nucleus membrane contact sites.The Journal of cell biology · 2024Article
- ENO1 promotes liver carcinogenesis through YAP1-dependent arachidonic acid metabolism.Nature chemical biology · 2023Article
- Mitochondrial Metabolism in the Spotlight: Maintaining Balanced RNAP III Activity Ensures Cellular Homeostasis.International journal of molecular sciences · 2023Article
- The Role of Genetic Mutations in Mitochondrial-Driven Cancer Growth in Selected Tumors: Breast and Gynecological Malignancies.Life (Basel, Switzerland) · 2023Review
- T-DNA insertion mutagenesis inMicrobiology (Reading, England) · 2023Article
- Small noncoding RNA interactome capture reveals pervasive, carbon source-dependent tRNA engagement of yeast glycolytic enzymes.RNA (New York, N.Y.) · 2023Article
- Oncometabolism: A Paradigm for the Metabolic Remodeling of the Failing Heart.International journal of molecular sciences · 2022Review
- The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation.RNA (New York, N.Y.) · 2022Review
- Circular RNA circNFKB1 promotes osteoarthritis progression through interacting with ENO1 and sustaining NF-κB signaling.Cell death & disease · 2022Article
- Mitochondrial Genome Editing to Treat Human Osteoarthritis-A Narrative Review.International journal of molecular sciences · 2022Review
- ENO1 suppresses cancer cell ferroptosis by degrading the mRNA of iron regulatory protein 1.Nature cancer · 2022Article
- The Diversity of the Mitochondrial Outer Membrane Protein Import Channels: Emerging Targets for Modulation.Molecules (Basel, Switzerland) · 2021Review
- Core Fermentation (CoFe) granules focus coordinated glycolytic mRNA localization and translation to fuel glucose fermentation.iScience · 2021Article
13 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In many organisms, mitochondria import nuclear DNA-encoded small RNAs. In yeast Saccharomyces cerevisiae, one out of two cytoplasmic isoacceptor tRNAs(Lys) is partially addressed into the organelle. Mitochondrial targeting of this tRNA was shown to depend on interaction with the precursor of mitochondrial lysyl-tRNA synthetase, preMsk1p. However, preMsk1p alone was unable to direct tRNA targeting, suggesting the existence of additional protein factor(s). Here, we identify the glycolytic enzyme, enolase, as such a factor. We demonstrate that recombinant enolase and preMSK1p are sufficient to direct tRNA import in vitro and that depletion of enolase inhibits tRNA import in vivo. Enzymatic and tRNA targeting functions of enolase appear to be independent. Three newly characterized properties of the enolase can be related to its novel function: (1) specific affinity to the imported tRNA, (2) the ability to facilitate formation of the complex between preMsk1p and the imported tRNA, and (3) partial targeting toward the mitochondrial outer membrane. We propose a model suggesting that the cell exploits mitochondrial targeting of the enolase in order to address the tRNA toward peri-mitochondrially synthesized preMsk1p. Our results indicate an alternative molecular chaperone function of glycolytic enzyme enolase in tRNA mitochondrial targeting.
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