Poster abstracts
Poster number 1 submitted by Sudeshi Abedeera
The h18pep1 inhibit RsuA binding to 16S rRNA
Sudeshi M. Abedeera (Department of Chemistry and Biochemistry, Kent State University), Jiale Xie (Department of Chemistry and Biochemistry, Kent State University), Sanjaya C. Abeysirigunawardena (Department of Chemistry and Biochemistry, Kent State University)
Abstract:
Ribosomes are an essential cellular component that carries out protein biosynthesis in all forms of life. Bacterial ribosome modification enzymes can have important biological roles other than their primary RNA modification function. Although many bacterial pseudouridine synthases are found to be non-essential for bacterial survival under normal growth conditions, their presence may be critical under non-conducing conditions such as environmental stress. Our studies illustrate that RsuA plays a crucial role in bacterial survival under streptomycin stress. Furthermore, the pseudouridylation activity of RsuA was observed to be important to render the survival advantage against streptomycin. We hypothesized that the efficacy of streptomycin as an antibiotic can be enhanced by blocking RsuA binding at helix18 thereby preventing the pseudouridylation at U516. We used phage display technique to discover a 12-mer peptide (h18pep1) that specifically binds to the same region of helix18 to which RsuA is known to interact. FRET-based assays were carried out using helix18 model RNA and 16S 5ยด-domain RNA to determine the ability of the selected 12-mer peptide to prevent RsuA binding to helix18. This work illustrates a useful strategy to combat antibiotic resistance in bacteria.
Keywords: Antibiotic resistance, Pseudouridine synthase, Streptomycin