Component

Human cytosolic tryptophanyl-tRNA synthetase / WARS1

Context-specific entity; species, compartment and exposure are stated on each claim.

2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

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What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. Under IFN-gamma/IDO1-associated tryptophan shortage, human cancer cells continued translation with WARS1-associated phenylalanine incorporation at tryptophan positions.

    Human cytosolic tryptophanyl-tRNA synthetase / WARS1 → Human cancer-cell tryptophan-to-phenylalanine translational substitution source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    evidence_access
    Primary abstract; primary correction full text reviewed
    experimental_model
    Human cancer-cell depletion, molecular assays and tumor proteomics.
    limitations
    Not a DNA mutation or a universal consequence of a low-tryptophan meal. Tumor proteomic filtering was clarified in a correction. Correction record: The 2022 author correction adds omitted funding acknowledgements and clarifies that the maximum-sample peptide filter was used in the intra-tumour analysis (Fig. 3f) but not for W>F substitutants in the tumour-specific analysis (Fig. 3a). Authors report similar biological conclusions with both strategies. This is a publication correction, not an opposing mechanism claim. https://www.nature.com/articles/s41586-022-05097-y
    nutrient_topic
    Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
    plain_language
    Severe local shortage can change what a cancer cell puts into a protein.
    primary_references
    Tryptophan depletion results in tryptophan-to-phenylalanine substitutants. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35264796/ · DOI 10.1038/s41586-022-04499-2
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 122–128

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human cancer-cell depletion, molecular assays and tumor proteomics. · source_derived_draft · unverified_draft

    ## tryptophan-w-to-f-shortage Severe local shortage can change what a cancer cell puts into a protein. Under IFN-gamma/IDO1-associated tryptophan shortage, human cancer cells continued translation with WARS1-associated phenylalanine incorporation at tryptophan positions. Model: Human cancer-cell depletion, molecular assays and tumor proteomics. Limitations: Not a DNA mutation or a universal consequence of a low-tryptophan meal. Tumor proteomic filtering was clarified in a correction. Correction record: The 2022 author correction adds omitted funding acknowledgements and clarifies that the maximum-sample peptide filter was used in the intra-tumour analysis (Fig. 3f) but not for W>F substitutants in the tumour-specific analysis (Fig. 3a). Authors report similar biological conclusions with both strategies. This is a publication correction, not an opposing mechanism claim. https://www.nature.com/articles/s41586-022-05097-y Evidence access: Primary abstract; primary correction full text reviewed Tryptophan depletion results in tryptophan-to-phenylalanine substitutants. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35264796/ · DOI 10.1038/s41586-022-04499-2
    Complete structured claim and evidence

  2. Human WARS1 recognizes tryptophan and its cognate tRNA; ATP-dependent activation precedes transfer to tRNA in protein-synthesis aminoacylation.

    Human cytosolic tryptophanyl-tRNA synthetase / WARS1 → Human tryptophanyl-tRNA-Trp source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text, aminoacylation mechanism and structural results
    experimental_model
    Human WARS1–tRNA structural analysis and biochemical aminoacylation.
    limitations
    Cytosolic WARS1 is distinct from mitochondrial WARS2.
    nutrient_topic
    Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
    plain_language
    Tryptophan is a building block that must be attached to the correct transfer RNA.
    primary_references
    Structure of human tryptophanyl-tRNA synthetase in complex with tRNATrp reveals the molecular basis of tRNA recognition and specificity. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16798914/ · DOI 10.1093/nar/gkl441

    Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 114–120

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human WARS1–tRNA structural analysis and biochemical aminoacylation. · source_derived_draft · unverified_draft

    ## tryptophan-wars1-charging Tryptophan is a building block that must be attached to the correct transfer RNA. Human WARS1 recognizes tryptophan and its cognate tRNA; ATP-dependent activation precedes transfer to tRNA in protein-synthesis aminoacylation. Model: Human WARS1–tRNA structural analysis and biochemical aminoacylation. Limitations: Cytosolic WARS1 is distinct from mitochondrial WARS2. Evidence access: Primary full text, aminoacylation mechanism and structural results Structure of human tryptophanyl-tRNA synthetase in complex with tRNATrp reveals the molecular basis of tRNA recognition and specificity. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16798914/ · DOI 10.1093/nar/gkl441
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards