ArticleThe Journal of biological chemistry2016
Molecular Basis and Consequences of the Cytochrome c-tRNA Interaction.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Genes near tRNAs are enriched in translational machinery.G3 (Bethesda, Md.) · 2026Article
- Genes near tRNAs are enriched in translational machinery.bioRxiv : the preprint server for biology · 2026Article
- Characterization of the interaction between human cytochromeMagnetic resonance letters · 2026Article
- Identification and experimental validation of prognostic genes related to cytochrome c in breast cancer.Frontiers in genetics · 2025Article
- Possible Roles of tRNA Fragments, as New Regulatory ncRNAs, in the Pathogenesis of Rheumatoid Arthritis.International journal of molecular sciences · 2021Review
- Noncanonical Roles of tRNAs: tRNA Fragments and Beyond.Annual review of genetics · 2020Review
- Exosomal microRNAs are novel circulating biomarkers in cigarette, waterpipe smokers, E-cigarette users and dual smokers.BMC medical genomics · 2020Article
- Hijacking tRNAs From Translation: Regulatory Functions of tRNAs in Mammalian Cell Physiology.Frontiers in molecular biosciences · 2020Review
- A genetically encoded fluorescent tRNA is active in live-cell protein synthesis.Nucleic acids research · 2017Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
The intrinsic apoptosis pathway occurs through the release of mitochondrial cytochrome c to the cytosol, where it promotes activation of the caspase family of proteases. The observation that tRNA binds to cytochrome c revealed a previously unexpected mode of apoptotic regulation. However, the molecular characteristics of this interaction, and its impact on each interaction partner, are not well understood. Using a novel fluorescence assay, we show here that cytochrome c binds to tRNA with an affinity comparable with other tRNA-protein binding interactions and with a molecular ratio of ∼3:1. Cytochrome c recognizes the tertiary structural features of tRNA, particularly in the core region. This binding is independent of the charging state of tRNA but is regulated by the redox state of cytochrome c. Compared with reduced cytochrome c, oxidized cytochrome c binds to tRNA with a weaker affinity, which correlates with its stronger pro-apoptotic activity. tRNA binding both facilitates cytochrome c reduction and inhibits the peroxidase activity of cytochrome c, which is involved in its release from mitochondria. Together, these findings provide new insights into the cytochrome c-tRNA interaction and apoptotic regulation.
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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.