Key result
Y-complex deletion impairs Bacillus subtilis ribosome degradation, increasing aggregated proteins by ~20% and reducing survival.
Why the study?
Limiting ribosome synthesis and activity is crucial for adapting to stresses, prompting a search for novel factors contributing to the heat shock response in Bacillus subtilis.
The Y-complex and RNase Y act as a regulatory hub in Bacillus subtilis to modulate gene expression and adjust protein synthesis during stress by degrading mature ribosomes.
Y-complex deletion heightens protein aggregation under bacterial stress; leaves open any role in eukaryotic or cardiovascular proteostasis.
Limiting the synthesis and activity of ribosomes is crucial for adaptation to stresses, such as heat or nutrient starvation. In Bacillus subtilis, this can be achieved through the coordinated action of the alarmones (p)ppGpp and the transcription factor Spx. Here, we performed a genetic screen to uncover novel factors contributing to the heat shock response of B. subtilis . We identified the Y-complex, which confers specificity to the endonuclease RNase Y, as a critical player during stress conditions, such as heat or transition into stationary phase. This protein complex is required for processing diverse RNAs, notably the maturation of mRNAs encoding proteins involved in translation and metabolism. We further demonstrate that the Y-complex and RNase Y initiate the degradation of rRNAs of mature ribosomes, lowering their abundance. We propose that the Y-complex is a regulatory hub that modulates gene expression, adjusts protein synthesis and resource allocation.
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Cornejo et al. (2025) studied Stress response in Bacillus subtilis. Y-complex deletion (ymcA, yaaT, ylbF) vs. Wild-type Bacillus subtilis was evaluated on Ribosome degradation and survival during heat shock. Deletion of the Y-complex in Bacillus subtilis impairs ribosome degradation during nutrient depletion and heat shock, leading to a 20% increase in aggregated proteins and reduced survival.
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