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iff-1

C. elegans

Eukaryotic translation initiation factor 5A;Eukaryotic translation initiation factor 5A-1;Translation elongation factor IF5A C-terminal domain-containing protein

What the model saw

Gene: iff-1
Organism: Caenorhabditis elegans
Known functions: Eukaryotic translation initiation factor 5A;Eukaryotic translation initiation factor 5A-1;Translation elongation factor IF5A C-terminal domain-containing protein. RNA binding. protein binding. ribosome binding. translation elongation factor activity.
View unredacted entry
Eukaryotic translation initiation factor 5A;Eukaryotic translation initiation factor 5A-1;Translation elongation factor IF5A C-terminal domain-containing protein. RNA binding. protein binding. ribosome binding. translation elongation factor activity.

Solver output

Predicted influence
Pro-longevity
Confidence
62%
Mechanism
Loss of proteostasis
Reasoning

iff-1 encodes the C. elegans ortholog of eukaryotic translation initiation/elongation factor 5A (eIF5A), which facilitates translation elongation at polyproline and other stalling sequences, and is uniquely activated by hypusination. Reduced eIF5A activity has been shown in multiple organisms to extend lifespan, likely by broadly dampening protein synthesis rates and reducing proteotoxic burden, consistent with the well-established pro-longevity effects of translation attenuation (e.g., via reduced ribosome activity or mTORC1 signaling). However, eIF5A also supports the translation of specific mRNAs including those encoding mitochondrial proteins and stress-response factors, so its normal function sustains robust protein synthesis. Because the normal (wild-type) function of iff-1 promotes active translation elongation, it opposes the translational slowdown associated with longevity; loss-of-function of eIF5A/iff-1 in C. elegans has been reported to extend lifespan, meaning the gene's normal activity is anti-longevity. Mechanistically, this maps to proteostasis: high translation rates driven by eIF5A increase the load on protein quality-control systems and can accelerate aging-associated proteotoxicity.

Key pathways
eIF5A-hypusination translation elongationmTORC1-regulated protein synthesisproteostasis network
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
Incorrect
Mechanism
Incorrect
Reasoning quality
2/5
Failure mode
Confident wrong
Notes

The model predicted "pro_longevity" but the ground truth is "anti_longevity". The model's reasoning is internally contradictory and confused. It starts by correctly noting that reduced eIF5A activity extends lifespan (which would make iff-1 anti_longevity), but then contradicts itself by concluding the gene is "pro_longevity." The model seems to conflate the direction of the effect: if loss-of-function extends lifespan, the gene is anti_longevity (its normal function opposes longevity), which is exactly what the ground truth says. The model even states "loss-of-function of eIF5A/iff-1 in C. elegans has been reported to extend lifespan, meaning the gene's normal activity is anti-longevity" — yet still outputs "pro_longevity" as its final answer. This is a clear logical error in the final classification despite partially correct mechanistic reasoning. The mechanism class of "loss_of_proteostasis" is also questionable; translation attenuation effects on longevity are more directly tied to protein synthesis rates and mTOR signaling rather than proteostasis per se.

Raw API responses

solver

{
  "reasoning": "iff-1 encodes the C. elegans ortholog of eukaryotic translation initiation/elongation factor 5A (eIF5A), which facilitates translation elongation at polyproline and other stalling sequences, and is uniquely activated by hypusination. Reduced eIF5A activity has been shown in multiple organisms to extend lifespan, likely by broadly dampening protein synthesis rates and reducing proteotoxic burden, consistent with the well-established pro-longevity effects of translation attenuation (e.g., via reduced ribosome activity or mTORC1 signaling). However, eIF5A also supports the translation of specific mRNAs including those encoding mitochondrial proteins and stress-response factors, so its normal function sustains robust protein synthesis. Because the normal (wild-type) function of iff-1 promotes active translation elongation, it opposes the translational slowdown associated with longevity; loss-of-function of eIF5A/iff-1 in C. elegans has been reported to extend lifespan, meaning the gene's normal activity is anti-longevity. Mechanistically, this maps to proteostasis: high translation rates driven by eIF5A increase the load on protein quality-control systems and can accelerate aging-associated proteotoxicity.",
  "confidence": 0.62,
  "key_pathways": [
    "eIF5A-hypusination translation elongation",
    "mTORC1-regulated protein synthesis",
    "proteostasis network"
  ],
  "mechanism_class": "loss_of_proteostasis",
  "longevity_influence": "pro_longevity"
}

advisor

{
  "notes": "The model predicted \"pro_longevity\" but the ground truth is \"anti_longevity\". The model's reasoning is internally contradictory and confused. It starts by correctly noting that reduced eIF5A activity extends lifespan (which would make iff-1 anti_longevity), but then contradicts itself by concluding the gene is \"pro_longevity.\" The model seems to conflate the direction of the effect: if loss-of-function extends lifespan, the gene is anti_longevity (its normal function opposes longevity), which is exactly what the ground truth says. The model even states \"loss-of-function of eIF5A/iff-1 in C. elegans has been reported to extend lifespan, meaning the gene's normal activity is anti-longevity\" — yet still outputs \"pro_longevity\" as its final answer. This is a clear logical error in the final classification despite partially correct mechanistic reasoning. The mechanism class of \"loss_of_proteostasis\" is also questionable; translation attenuation effects on longevity are more directly tied to protein synthesis rates and mTOR signaling rather than proteostasis per se.",
  "failure_mode": "confident_wrong",
  "answer_correct": false,
  "mechanism_correct": false,
  "reasoning_quality": 2,
  "ground_truth_questionable": false
}