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The mycobacterial ribosome is a 70S ribonucleoprotein complex composed of a small (30S) and large (50S) subunit, each assembled from unique ribosomal RNAs and proteins. While its fundamental role in protein translation is conserved across bacteria, recent high-resolution structures have shown distinct features characteristic to mycobacteria, such as unique extensions in rRNAs and ribosomal proteins (e.g., H54a insertion, bL27 interactions, and mycobacteria-specific proteins like bS22 and bL37)[1][3][4]. These adaptations affect translation dynamics, stress responses, and contribute to mechanisms like ribosome hibernation during dormancy—facilitated by factors such as RafH (a hypoxia-induced hibernation-promoting factor), which protects the ribosome and modifies susceptibility to antibiotic inhibitors[2][3][5]. These species-specific structural differences not only underpin essential survival pathways in pathogenic mycobacteria but also provide selective targets for antimycobacterial drug design.
Inhibition of protein synthesis by binding to ribosomal RNA or proteins, blocking initiation, elongation, or termination steps; Inducing ribosome stalling or dysfunction
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