RPL22A
S. cerevisiae
60S ribosomal protein eL22 RPL22A
What the model saw
Gene: RPL22A Organism: Saccharomyces cerevisiae Known functions: 60S ribosomal protein eL22 RPL22A. RNA binding. structural constituent of ribosome.
View unredacted entry
60S ribosomal protein eL22 RPL22A. RNA binding. structural constituent of ribosome.
Solver output
RPL22A encodes the 60S ribosomal protein eL22, a structural component of the large ribosomal subunit involved in RNA binding and ribosome assembly. Ribosomal proteins are core effectors of translational capacity, which is tightly coupled to TOR (Target of Rapamycin) nutrient-sensing signaling in yeast. Elevated ribosome biogenesis and translation activity downstream of TORC1 is a well-established driver of aging in S. cerevisiae, and deletion of many large ribosomal subunit genes extends chronological and replicative lifespan. Specifically, reduced 60S ribosomal protein levels dampen global protein synthesis rates, mimicking dietary restriction and attenuating pro-aging anabolic signaling. Loss-of-function of RPL22A (and its paralog RPL22B) has been associated with lifespan extension in yeast, consistent with the broader pattern that ribosomal protein gene deletions are among the most enriched longevity-extending interventions in genome-wide screens. Therefore, the normal function of RPL22A—promoting ribosome assembly and translation—opposes longevity.
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 RPL22A. The mechanistic reasoning is sound: ribosomal protein deletions in yeast commonly extend lifespan by reducing translational capacity, mimicking dietary restriction, and attenuating TORC1-driven anabolic signaling. The model correctly identifies that RPL22A's normal function (promoting ribosome assembly and translation) opposes longevity, making it anti-longevity. The mechanism class "deregulated_nutrient_sensing" is a reasonable fit, though "translational regulation" might be more precise. The reasoning is well-supported and consistent with the broader literature on ribosomal protein deletions extending yeast lifespan. Confidence of 0.65 is appropriately calibrated given the complexity of the field.
Raw API responses
solver
{
"reasoning": "RPL22A encodes the 60S ribosomal protein eL22, a structural component of the large ribosomal subunit involved in RNA binding and ribosome assembly. Ribosomal proteins are core effectors of translational capacity, which is tightly coupled to TOR (Target of Rapamycin) nutrient-sensing signaling in yeast. Elevated ribosome biogenesis and translation activity downstream of TORC1 is a well-established driver of aging in S. cerevisiae, and deletion of many large ribosomal subunit genes extends chronological and replicative lifespan. Specifically, reduced 60S ribosomal protein levels dampen global protein synthesis rates, mimicking dietary restriction and attenuating pro-aging anabolic signaling. Loss-of-function of RPL22A (and its paralog RPL22B) has been associated with lifespan extension in yeast, consistent with the broader pattern that ribosomal protein gene deletions are among the most enriched longevity-extending interventions in genome-wide screens. Therefore, the normal function of RPL22A—promoting ribosome assembly and translation—opposes longevity.",
"confidence": 0.65,
"key_pathways": [
"TORC1-driven ribosome biogenesis",
"translational regulation and protein synthesis",
"60S ribosomal subunit assembly"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "anti_longevity"
}advisor
{
"notes": "The model correctly predicted anti_longevity for RPL22A. The mechanistic reasoning is sound: ribosomal protein deletions in yeast commonly extend lifespan by reducing translational capacity, mimicking dietary restriction, and attenuating TORC1-driven anabolic signaling. The model correctly identifies that RPL22A's normal function (promoting ribosome assembly and translation) opposes longevity, making it anti-longevity. The mechanism class \"deregulated_nutrient_sensing\" is a reasonable fit, though \"translational regulation\" might be more precise. The reasoning is well-supported and consistent with the broader literature on ribosomal protein deletions extending yeast lifespan. Confidence of 0.65 is appropriately calibrated given the complexity of the field.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 4,
"ground_truth_questionable": false
}