The Bacteroidetes represent an important group of bacteria, well represented in intestinal tracts of mammals, including humans. Gene expression in the Bacteroidetes differs substantially from that of well-studied bacteria, such as Escherichia coli. This project will reveal the distinct manner in which proteins are made in the Bacteroidetes. The knowledge gained may spur advances in biotechnology and medicine. This project will also provide (i) research training for undergraduate, graduate, and postdoctoral students, (ii) summer research opportunities for local high school students (Columbus Public Schools), and (iii) mentorship training for junior faculty at Ohio State University.
In all cells, ribosomes translate the genetic code, synthesizing proteins based on the information content of mRNA. The rate of translation varies dramatically, depending on the translation initiation region (TIR) of mRNA. How intrinsic features of the TIR govern the rate of translation initiation remains an important open question. In bacteria such as E. coli, one well-known feature of the TIR is the Shine-Dalgarno (SD) sequence, a purine-rich element that lies just upstream from the start codon. The SD pairs with the anti-SD (ASD), a pyrimidine-rich element at the 3? end of the 16S rRNA, to promote initiation. Recent studies have shown that certain taxonomic groups of bacteria, such as the Bacteroidetes, lack SD sequences in their mRNA. Yet, their ribosomes retain the conserved ASD. The project aims to elucidate the unique aspects of protein synthesis in the Bacteroidetes, using Flavobacterium johnsoniae as a model organism. Specifically, the work will address (i) which components of the ribosome govern ASD-mRNA pairing, (ii) how initiation complex formation occurs in F. johnsoniae, (iii) whether the ASD plays a role in ribosome assembly, and (iv) how autoregulation of release factor RF2 occurs in F. johnsoniae. The results will provide fundamental insight on mechanisms of translation initiation, programmed frameshifting, and ribosome assembly in diverse bacteria.
This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.
