L2 is essential for ribosome assembly and catalytic function:
Subunit Association: Facilitates the docking of 30S and 50S subunits to form the 70S ribosome, a prerequisite for translation initiation.
tRNA Binding: Stabilizes tRNA interactions at the A and P sites, particularly at the tRNA elbow region.
Peptidyl-Transferase Activity: Contributes to peptide bond formation, though controversy exists about its direct catalytic role.
In E. coli, L2 interacts with the RNA polymerase α-subunit to modulate transcription at ribosomal promoters. While not directly studied in Bdellovibrio, this suggests a potential regulatory link between translation and transcription.
Mutations in L2 (e.g., His229 substitutions) confer resistance to bactobolins, a novel antibiotic class targeting the 50S subunit. This highlights L2 as a potential therapeutic target.
Recombinant Bdellovibrio bacteriovorus 50S ribosomal protein L2 (rplB) is a key rRNA-binding protein. It's essential for the association of 30S and 50S ribosomal subunits to form the 70S ribosome, facilitating tRNA binding and peptide bond formation. While some evidence suggests peptidyltransferase activity, this remains somewhat controversial. The protein establishes multiple contacts with the 16S rRNA within the 70S ribosome.
KEGG: bba:Bd2973
STRING: 264462.Bd2973