Ribosomal allostery as a potential regulator of bacterial dormancy

Area of Science:

• Molecular Biology
• Biochemistry
• Structural Biology

Background:

• Ribosomes are essential for protein synthesis.
• Ribosomes also integrate cellular stress responses.
• Ribosomal protein L11's role in these processes is not fully understood.

Purpose of the Study:

• To investigate how ribosomal protein L11 regulates ribosome conformational dynamics.
• To understand the role of L11 in long-distance communication within the ribosome.
• To examine the physiological implications of L11 deletion on bacterial stress adaptation.

Main Methods:

• Long-timescale molecular dynamics simulations of wild-type and L11-deleted ribosomes.
• Construction and analysis of a ΔL11 Bacillus subtilis strain.
• Quantification of sporulation behavior in the ΔL11 strain.

Main Results:

• L11 acts as a global allosteric regulator, coordinating communication between the ribosomal stalk and the peptidyl transferase center.
• L11 deletion disrupts long-distance couplings and rigidifies the hibernation-promoting factor site.
• The ΔL11 strain shows delayed entry into and exit from dormancy, indicating impaired stress-adaptive ribosomal regulation.

Conclusions:

• Ribosomal protein L11 is crucial for maintaining ribosome conformational dynamics and allosteric regulation.
• L11 plays a key role in bacterial stress adaptation and survival by modulating ribosome function.
• Understanding L11's function provides insights into how local ribosomal changes impact global physiology and bacterial persistence under stress.