rpl-31
C. elegans
Large ribosomal subunit protein eL31
What the model saw
Gene: rpl-31 Organism: Caenorhabditis elegans Known functions: Large ribosomal subunit protein eL31. structural constituent of ribosome.
View unredacted entry
Large ribosomal subunit protein eL31. structural constituent of ribosome.
Solver output
rpl-31 encodes the large ribosomal subunit protein eL31, a structural component of the 60S ribosomal subunit. Ribosomal proteins are core effectors of the TOR (Target of Rapamycin) nutrient-sensing pathway, which couples nutrient availability to translational capacity. In C. elegans, reduced ribosomal function — through partial loss-of-function of large subunit proteins — is well established to extend lifespan, likely by attenuating global translation rates and mimicking dietary restriction or TOR inhibition. Downregulation of multiple large ribosomal subunit proteins (e.g., rpl-11.1, rpl-25.1) extends worm lifespan, placing rpl-31's normal pro-translational function in opposition to longevity. The mechanism likely involves reduced proteotoxic burden and improved proteostasis as secondary consequences of lower translational output, but the primary driver is nutrient/TOR-coupled ribosome biogenesis and activity.
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
The model correctly predicted anti_longevity for rpl-31. The mechanistic reasoning is sound: ribosomal large subunit proteins like rpl-31 are anti-longevity because their knockdown reduces translation rates, mimicking TOR inhibition/dietary restriction and extending lifespan. The model correctly identifies that the normal function of rpl-31 (promoting translation) opposes longevity, making it anti-longevity. The mechanism class "deregulated_nutrient_sensing" is a reasonable framing, though "translational regulation" might be more precise as the primary mechanism. The reasoning is well-supported by known C. elegans biology. Confidence of 0.72 is appropriate given the general knowledge about ribosomal proteins in aging.
Raw API responses
solver
{
"reasoning": "rpl-31 encodes the large ribosomal subunit protein eL31, a structural component of the 60S ribosomal subunit. Ribosomal proteins are core effectors of the TOR (Target of Rapamycin) nutrient-sensing pathway, which couples nutrient availability to translational capacity. In C. elegans, reduced ribosomal function — through partial loss-of-function of large subunit proteins — is well established to extend lifespan, likely by attenuating global translation rates and mimicking dietary restriction or TOR inhibition. Downregulation of multiple large ribosomal subunit proteins (e.g., rpl-11.1, rpl-25.1) extends worm lifespan, placing rpl-31's normal pro-translational function in opposition to longevity. The mechanism likely involves reduced proteotoxic burden and improved proteostasis as secondary consequences of lower translational output, but the primary driver is nutrient/TOR-coupled ribosome biogenesis and activity.",
"confidence": 0.72,
"key_pathways": [
"TOR signaling / ribosome biogenesis",
"translational regulation",
"dietary restriction mimicry"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "anti_longevity"
}advisor
{
"notes": "The model correctly predicted anti_longevity for rpl-31. The mechanistic reasoning is sound: ribosomal large subunit proteins like rpl-31 are anti-longevity because their knockdown reduces translation rates, mimicking TOR inhibition/dietary restriction and extending lifespan. The model correctly identifies that the normal function of rpl-31 (promoting translation) opposes longevity, making it anti-longevity. The mechanism class \"deregulated_nutrient_sensing\" is a reasonable framing, though \"translational regulation\" might be more precise as the primary mechanism. The reasoning is well-supported by known C. elegans biology. Confidence of 0.72 is appropriate given the general knowledge about ribosomal proteins in aging.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 4,
"ground_truth_questionable": false
}