Ribosomal allostery as a potential regulator of bacterial dormancy.

Ribosomes are central to protein synthesis but also serve as dynamic hubs that integrate cellular stress responses. Here, we investigate how ribosomal protein L11 regulates ribosome conformational dynamics and long-distance coupling. Long-timescale molecular dynamics simulations of wild-type and L11-deleted (ΔL11) ribosomes reveal that L11 functions as a global allosteric regulator coordinating communication between the ribosomal stalk and the peptidyl transferase center. The absence of L11 disrupts long-distance couplings involving RelA and Obg and rigidifies the hibernation-promoting factor site, suggesting altered hibernation dynamics that could affect ribosome persistence under stress. To examine the physiological implications of these computational predictions, we construct a ΔL11 Bacillus subtilis strain and quantify its sporulation behavior. The ΔL11 variant exhibits delayed entry into and exit from dormancy, consistent with a breakdown in stress-adaptive ribosomal regulation. Overall, these results highlight the role of L11 in ribosomal allostery, suggesting how local perturbations propagate through the ribosome to influence global physiological outcomes and bacterial survival under environmental stress.