Poster abstracts
Poster number 3 submitted by Md Siddik Alom
Ribosomal protein bL38, a uniquely conserved component of the Bacteroidia ribosome
Md Siddik Alom (Ohio State Biochemistry Program, Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA), Zakkary A. McNutt (Ohio State Biochemistry Program, Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA), Kurt L. Fredrick (Ohio State Biochemistry Program, Center for RNA Biology, Department of Microbiology The Ohio State University, Columbus, OH 43210, USA)
Abstract:
Flavobacterium johnsoniae is an aerobic bacterium that belongs to class Bacteroidia. Recent biochemical and structural analyses of the F. johnsoniae ribosome revealed a novel protein of the large subunit, bL38, a 5.6 kDa protein encoded downstream of the bL28 and bL33 genes, in a three-gene operon. This protein is conserved across the Bacteroidia but absent in other organisms. To understand the function of bL38, we have engineered a conditional strain, which contains an in-frame deletion of the rpmL (bL38) gene and a covering plasmid with rpmL downstream under an inducible promoter. Using this strain, we have shown that the growth of F. johnsoniae depends on production of the bL38 protein. Moreover, depletion of bL38 leads to accumulation of ribosomal subunits, consistent with defect in 50S assembly. Based on our findings, we propose that bL38 interactions with uL6 are important for 50S subunit assembly and/or stability in the Bacteroidia.
Keywords: bL38, F johnsoniae, ribosome