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rpl-30

C. elegans

Large ribosomal subunit protein eL30

What the model saw

Gene: rpl-30
Organism: Caenorhabditis elegans
Known functions: Large ribosomal subunit protein eL30. RNA binding. structural constituent of ribosome.
View unredacted entry
Large ribosomal subunit protein eL30. RNA binding. structural constituent of ribosome.

Solver output

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

rpl-30 encodes the large ribosomal subunit protein eL30, a structural component of the 60S ribosomal subunit required for mRNA translation. Ribosomal protein genes are downstream effectors of the TOR (Target of Rapamycin) nutrient-sensing pathway, which promotes global protein synthesis. In C. elegans, reduced ribosomal activity — through RNAi knockdown of large subunit proteins or partial loss-of-function — is well established to extend lifespan, as it mimics dietary restriction and dampens TOR-driven anabolic signaling. The normal function of rpl-30 thus sustains high translational capacity, which is associated with accelerated aging. Additionally, reduced ribosome biogenesis and translation fidelity improvements under low ribosomal activity can enhance proteostasis and stress resistance, further supporting the anti-longevity role of full rpl-30 activity.

Key pathways
TOR/mTORC1 nutrient-sensing and translational control60S ribosome biogenesis and global protein synthesisdietary restriction mimicry via ribosomal attenuation
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 rpl-30. The mechanistic reasoning is sound: ribosomal large subunit proteins like eL30 support high translational capacity downstream of TOR signaling, and their knockdown in C. elegans is well-documented to extend lifespan by mimicking dietary restriction. The mechanism class "deregulated_nutrient_sensing" is a reasonable fit, though "translational regulation" might be more precise. The reasoning about proteostasis improvements under reduced ribosomal activity is also valid. Overall, solid prediction with good mechanistic understanding.

Raw API responses

solver

{
  "reasoning": "rpl-30 encodes the large ribosomal subunit protein eL30, a structural component of the 60S ribosomal subunit required for mRNA translation. Ribosomal protein genes are downstream effectors of the TOR (Target of Rapamycin) nutrient-sensing pathway, which promotes global protein synthesis. In C. elegans, reduced ribosomal activity — through RNAi knockdown of large subunit proteins or partial loss-of-function — is well established to extend lifespan, as it mimics dietary restriction and dampens TOR-driven anabolic signaling. The normal function of rpl-30 thus sustains high translational capacity, which is associated with accelerated aging. Additionally, reduced ribosome biogenesis and translation fidelity improvements under low ribosomal activity can enhance proteostasis and stress resistance, further supporting the anti-longevity role of full rpl-30 activity.",
  "confidence": 0.72,
  "key_pathways": [
    "TOR/mTORC1 nutrient-sensing and translational control",
    "60S ribosome biogenesis and global protein synthesis",
    "dietary restriction mimicry via ribosomal attenuation"
  ],
  "mechanism_class": "deregulated_nutrient_sensing",
  "longevity_influence": "anti_longevity"
}

advisor

{
  "notes": "The model correctly predicted anti_longevity for rpl-30. The mechanistic reasoning is sound: ribosomal large subunit proteins like eL30 support high translational capacity downstream of TOR signaling, and their knockdown in C. elegans is well-documented to extend lifespan by mimicking dietary restriction. The mechanism class \"deregulated_nutrient_sensing\" is a reasonable fit, though \"translational regulation\" might be more precise. The reasoning about proteostasis improvements under reduced ribosomal activity is also valid. Overall, solid prediction with good mechanistic understanding.",
  "failure_mode": "correct",
  "answer_correct": true,
  "mechanism_correct": true,
  "reasoning_quality": 4,
  "ground_truth_questionable": false
}