Component
Human mitochondrial cysteinyl-tRNA synthetase / CARS2
Context-specific entity; species, compartment and exposure are stated on each claim.
3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What it acts on
CARS2-deficient human cells had fragmented or shrunken mitochondria; re-expression of wild-type or persulfide-competent C78/257D CARS2 improved morphology, unlike the tested persulfide-impaired lysine mutants.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary full text
- experimental_model
- Human HEK293T imaging and mutant rescue.
- limitations
- This does not show that free-cysteine supplementation repairs mitochondrial disease.
- nutrient_topic
- L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
- plain_language
- Sulfur chemistry contributed to mitochondrial behavior beyond protein production.
- primary_references
- Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. · 2017 · https://pubmed.ncbi.nlm.nih.gov/29079736/ · DOI 10.1038/s41467-017-01311-y
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 172–178
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human HEK293T imaging and mutant rescue. · source_derived_draft · unverified_draft
## l-cysteine-cars2-mitochondrial-shape Sulfur chemistry contributed to mitochondrial behavior beyond protein production. CARS2-deficient human cells had fragmented or shrunken mitochondria; re-expression of wild-type or persulfide-competent C78/257D CARS2 improved morphology, unlike the tested persulfide-impaired lysine mutants. Model: Human HEK293T imaging and mutant rescue. Limitations: This does not show that free-cysteine supplementation repairs mitochondrial disease. Evidence access: Primary full text Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. · 2017 · https://pubmed.ncbi.nlm.nih.gov/29079736/ · DOI 10.1038/s41467-017-01311-y
Complete structured claim and evidenceCARS2 disruption lowered cysteine-persulfide production in human cells, and wild-type or the C78/257D mutant restored it despite differing effects on translation.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary full text
- experimental_model
- Human HEK293T knockout/rescue and LC–MS/MS persulfide assays.
- limitations
- Assay and mutation-dependent evidence; the proposed importance of this route is not proof of identical dominance in all human tissues.
- nutrient_topic
- L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
- plain_language
- One enzyme had separable roles in protein synthesis and sulfur chemistry.
- primary_references
- Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. · 2017 · https://pubmed.ncbi.nlm.nih.gov/29079736/ · DOI 10.1038/s41467-017-01311-y
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 164–170
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human HEK293T knockout/rescue and LC–MS/MS persulfide assays. · source_derived_draft · unverified_draft
## l-cysteine-cars2-persulfide One enzyme had separable roles in protein synthesis and sulfur chemistry. CARS2 disruption lowered cysteine-persulfide production in human cells, and wild-type or the C78/257D mutant restored it despite differing effects on translation. Model: Human HEK293T knockout/rescue and LC–MS/MS persulfide assays. Limitations: Assay and mutation-dependent evidence; the proposed importance of this route is not proof of identical dominance in all human tissues. Evidence access: Primary full text Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. · 2017 · https://pubmed.ncbi.nlm.nih.gov/29079736/ · DOI 10.1038/s41467-017-01311-y
Complete structured claim and evidenceCARS2 disruption reduced mitochondrial cysteinyl-tRNA synthetase function, assessed in part through mitochondrial MTCO1 expression; mutant rescue distinguished this from persulfide synthesis.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary full text
- experimental_model
- Human HEK293T CARS2-deficient cells and C78/257D versus lysine-motif mutant complementation.
- limitations
- MTCO1 expression is a translation-related readout, not a direct measurement of dietary cysteine incorporation.
- nutrient_topic
- L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
- plain_language
- Mitochondria need their own enzyme to place cysteine into proteins.
- primary_references
- Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. · 2017 · https://pubmed.ncbi.nlm.nih.gov/29079736/ · DOI 10.1038/s41467-017-01311-y
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 156–162
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human HEK293T CARS2-deficient cells and C78/257D versus lysine-motif mutant complementation. · source_derived_draft · unverified_draft
## l-cysteine-cars2-translation Mitochondria need their own enzyme to place cysteine into proteins. CARS2 disruption reduced mitochondrial cysteinyl-tRNA synthetase function, assessed in part through mitochondrial MTCO1 expression; mutant rescue distinguished this from persulfide synthesis. Model: Human HEK293T CARS2-deficient cells and C78/257D versus lysine-motif mutant complementation. Limitations: MTCO1 expression is a translation-related readout, not a direct measurement of dietary cysteine incorporation. Evidence access: Primary full text Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. · 2017 · https://pubmed.ncbi.nlm.nih.gov/29079736/ · DOI 10.1038/s41467-017-01311-y
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.