50S ribosomal protein L28 (rpmB) is a structural component of the large ribosomal subunit, critical for ribosome assembly and protein synthesis. In Bacteroides thetaiotaomicron, this protein is encoded by the rpmB gene. Homologs in other bacteria, such as Escherichia coli and Stenotrophomonas maltophilia, demonstrate that L28 is essential for proper 50S subunit formation. For example, deletion of rpmB in E. coli prevents 70S ribosome assembly, leading to accumulation of defective 47S particles .
Ribosome Assembly: L28 is indispensable for 50S subunit maturation. In E. coli, its absence results in incomplete ribosomal particles lacking L28 and L33 .
Oxidative Stress Link: B. thetaiotaomicron’s metabolic adaptations under oxidative stress involve ribosomal machinery. While L28’s direct role is unstudied, rhamnose metabolism upregulates stress-response genes (e.g., rhaR), suggesting ribosomal proteins may indirectly stabilize translation under stress .
Functional Characterization: No studies directly address B. thetaiotaomicron L28’s role in ribosome assembly or stress responses.
Interactome Analysis: Potential interactions with oxidative stress regulators (e.g., RhaR) or novel small proteins (DUF4295) remain uninvestigated .
Structural Studies: Cryo-EM or X-ray crystallography of B. thetaiotaomicron ribosomes could resolve L28’s spatial role.