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eif-3.F

C. elegans

Eukaryotic translation initiation factor 3 subunit F

What the model saw

Gene: eif-3.F
Organism: Caenorhabditis elegans
Known functions: Eukaryotic translation initiation factor 3 subunit F. metal-dependent deubiquitinase activity. metallopeptidase activity. peptidase activity. translation initiation factor activity. translation initiation factor binding.
View unredacted entry
Eukaryotic translation initiation factor 3 subunit F. metal-dependent deubiquitinase activity. metallopeptidase activity. peptidase activity. translation initiation factor activity. translation initiation factor binding.

Solver output

Predicted influence
Anti-longevity
Confidence
72%
Mechanism
Deregulated nutrient sensing
Reasoning

eif-3.F encodes subunit F of the eukaryotic translation initiation factor 3 (eIF3) complex, which is a core component of the 43S pre-initiation complex that drives cap-dependent mRNA translation. Elevated global translation rates are a well-established driver of aging in C. elegans; RNAi knockdown of multiple eIF3 subunits and other translation initiation factors extends lifespan, consistent with the idea that reducing protein synthesis mimics dietary restriction and activates longevity pathways downstream of TOR/TORC1 signaling. The eIF3 complex is a major effector of mTORC1-stimulated translation, placing eif-3.F squarely within the deregulated nutrient-sensing hallmark. Additionally, the metal-dependent deubiquitinase/metallopeptidase activity of this subunit may modulate proteasomal or ubiquitin-mediated regulation of translation factors, but the dominant pro-growth, pro-translation function is expected to be the primary aging-relevant activity. Thus, normal function of eif-3.F promotes translation and opposes longevity.

Key pathways
mTORC1-driven cap-dependent translation initiationeIF3 complex assembly and ribosome recruitmentTOR/nutrient-sensing longevity pathway
Longevity influence
Anti-longevity
Lifespan effect
Increase

GenAge curators classify each gene's normal function as promoting (Pro-Longevity) or opposing (Anti-Longevity) longevity, based on synthesis across studies. Loss-of-function effects can vary from this depending on the manipulation.

Advisor judgment

Answer
Correct
Mechanism
Correct
Reasoning quality
4/5
Failure mode
Correct
Notes

The model correctly predicted anti_longevity for eif-3.F with good confidence (0.72). The mechanistic reasoning is sound: eIF3 subunits promote global translation, and reducing translation via RNAi knockdown of eIF3 subunits extends lifespan in C. elegans, consistent with TOR/nutrient-sensing pathway involvement. The model also correctly noted the metal-dependent deubiquitinase activity as a secondary consideration. The mechanism class "deregulated_nutrient_sensing" is reasonable given the mTORC1-translation axis, though one could argue "altered translation" might be more precise. Overall, the reasoning is well-grounded in established C. elegans aging biology.

Raw API responses

solver

{
  "reasoning": "eif-3.F encodes subunit F of the eukaryotic translation initiation factor 3 (eIF3) complex, which is a core component of the 43S pre-initiation complex that drives cap-dependent mRNA translation. Elevated global translation rates are a well-established driver of aging in C. elegans; RNAi knockdown of multiple eIF3 subunits and other translation initiation factors extends lifespan, consistent with the idea that reducing protein synthesis mimics dietary restriction and activates longevity pathways downstream of TOR/TORC1 signaling. The eIF3 complex is a major effector of mTORC1-stimulated translation, placing eif-3.F squarely within the deregulated nutrient-sensing hallmark. Additionally, the metal-dependent deubiquitinase/metallopeptidase activity of this subunit may modulate proteasomal or ubiquitin-mediated regulation of translation factors, but the dominant pro-growth, pro-translation function is expected to be the primary aging-relevant activity. Thus, normal function of eif-3.F promotes translation and opposes longevity.",
  "confidence": 0.72,
  "key_pathways": [
    "mTORC1-driven cap-dependent translation initiation",
    "eIF3 complex assembly and ribosome recruitment",
    "TOR/nutrient-sensing longevity pathway"
  ],
  "mechanism_class": "deregulated_nutrient_sensing",
  "longevity_influence": "anti_longevity"
}

advisor

{
  "notes": "The model correctly predicted anti_longevity for eif-3.F with good confidence (0.72). The mechanistic reasoning is sound: eIF3 subunits promote global translation, and reducing translation via RNAi knockdown of eIF3 subunits extends lifespan in C. elegans, consistent with TOR/nutrient-sensing pathway involvement. The model also correctly noted the metal-dependent deubiquitinase activity as a secondary consideration. The mechanism class \"deregulated_nutrient_sensing\" is reasonable given the mTORC1-translation axis, though one could argue \"altered translation\" might be more precise. Overall, the reasoning is well-grounded in established C. elegans aging biology.",
  "failure_mode": "correct",
  "answer_correct": true,
  "mechanism_correct": true,
  "reasoning_quality": 4,
  "ground_truth_questionable": false
}