Key result
Hibernation-promoting factor (HPF) from Bacillus subtilis preserves ribosomes by preventing the loss of essential ribosomal proteins at the dimer interface during periods of dormancy.
HPF-mediated ribosome dimerization protects the small ribosomal subunit from losing essential proteins during dormancy, aiding survival during nutrient limitation.
Should not yet change practice; leaves open ribosome preservation strategies in human pathogens or stressed cardiac cells.
The formation of ribosome dimers during periods of dormancy is widespread among bacteria. Dimerization is typically mediated by a single protein, hibernation-promoting factor (HPF). Bacteria lacking HPF exhibit strong defects in viability and pathogenesis and, in some species, extreme loss of rRNA. The mechanistic basis of these phenotypes has not been determined. Here, we report that HPF from the Gram-positive bacterium Bacillus subtilis preserves ribosomes by preventing the loss of essential ribosomal proteins at the dimer interface. This protection may explain phenotypes associated with the loss of HPF, since ribosome protection would aid survival during nutrient limitation and impart a strong selective advantage when the bacterial cell rapidly reinitiates growth in the presence of sufficient nutrients.
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Feaga et al. (2020) studied Bacterial dormancy. Hibernation-promoting factor (HPF) vs. Bacteria lacking HPF was evaluated on Preservation of ribosomes and prevention of loss of essential ribosomal proteins. Hibernation-promoting factor (HPF) from Bacillus subtilis preserves ribosomes by preventing the loss of essential ribosomal proteins at the dimer interface during periods of dormancy.
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