RPL23A
S. cerevisiae
60S ribosomal protein uL14 RPL23A
What the model saw
Gene: RPL23A Organism: Saccharomyces cerevisiae Known functions: 60S ribosomal protein uL14 RPL23A. large ribosomal subunit rRNA binding. structural constituent of ribosome.
View unredacted entry
60S ribosomal protein uL14 RPL23A. large ribosomal subunit rRNA binding. structural constituent of ribosome.
Solver output
RPL23A encodes a structural component of the 60S large ribosomal subunit (uL14) that binds rRNA and is essential for ribosome assembly and translational capacity. In yeast, ribosome biogenesis is a major downstream effector of the TOR (Target of Rapamycin) nutrient-sensing pathway; high ribosomal activity is associated with active TOR signaling, which is pro-growth but anti-longevity. Deletion of large ribosomal subunit proteins, including RPL23A, has been shown to extend chronological and replicative lifespan in S. cerevisiae, likely by mimicking TOR inhibition and reducing global translation rates. Reduced translational output decreases proteotoxic burden and may upregulate stress-response and autophagy programs. Thus, the normal (wild-type) function of RPL23A — promoting full ribosomal activity — opposes longevity by sustaining high TOR-driven translation.
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 RPL23A. The mechanistic reasoning is sound and well-articulated: RPL23A encodes a 60S ribosomal subunit protein, and deletion of large ribosomal subunit proteins in yeast is well-established to extend lifespan by reducing translational output and mimicking TOR inhibition. The model correctly identifies the TOR/ribosome biogenesis axis as the key pathway, and appropriately frames the wild-type function as anti-longevity (promoting high translation rates). Confidence of 0.72 is reasonable given the general knowledge about ribosomal protein deletions in yeast longevity studies.
Raw API responses
solver
{
"reasoning": "RPL23A encodes a structural component of the 60S large ribosomal subunit (uL14) that binds rRNA and is essential for ribosome assembly and translational capacity. In yeast, ribosome biogenesis is a major downstream effector of the TOR (Target of Rapamycin) nutrient-sensing pathway; high ribosomal activity is associated with active TOR signaling, which is pro-growth but anti-longevity. Deletion of large ribosomal subunit proteins, including RPL23A, has been shown to extend chronological and replicative lifespan in S. cerevisiae, likely by mimicking TOR inhibition and reducing global translation rates. Reduced translational output decreases proteotoxic burden and may upregulate stress-response and autophagy programs. Thus, the normal (wild-type) function of RPL23A — promoting full ribosomal activity — opposes longevity by sustaining high TOR-driven translation.",
"confidence": 0.72,
"key_pathways": [
"TOR signaling / ribosome biogenesis",
"translational regulation",
"60S ribosomal subunit assembly"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "anti_longevity"
}advisor
{
"notes": "The model correctly predicted anti_longevity for RPL23A. The mechanistic reasoning is sound and well-articulated: RPL23A encodes a 60S ribosomal subunit protein, and deletion of large ribosomal subunit proteins in yeast is well-established to extend lifespan by reducing translational output and mimicking TOR inhibition. The model correctly identifies the TOR/ribosome biogenesis axis as the key pathway, and appropriately frames the wild-type function as anti-longevity (promoting high translation rates). Confidence of 0.72 is reasonable given the general knowledge about ribosomal protein deletions in yeast longevity studies.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 5,
"ground_truth_questionable": false
}