Poster abstracts
Poster number 41 submitted by Ashanti Matlock
Investigating the biological roles for thg1-like proteins in Myxococcus xanthus
Ashanti Matlock (Chemistry and Biochemistry), Jane Jackman (Chemistry and Biochemistry)
Abstract:
The tRNAHis guanylyltransferase (Thg1) enzyme family is a unique group of proteins that catalyze 3' to 5' nucleotide addition. The biological function of 3' to 5' nucleotide addition catalyzed by Thg1 in eukaryotes is to add a single essential guanine to the 5' end of tRNAHis. By modifying tRNAHis with an additional guanine at the -1 position, Thg1 insures translational fidelity by guaranteeing proper charging by histidyl amino acyl synthetase. Conversely, the biological significance of TLPs in bacteria and archaea is less clear. It is likely that TLPs are not used for tRNAHis maturation because G-1 is predicted to be retained in the mature transcript after 5' end processing by RNase P. Possible functions for TLPs include 5' end repair of truncated mitochondrial tRNAs, as recently demonstrated in Dictyostelium discoideum. However, biological roles for bacterial TLPs remain elusive due to the difficulty of obtaining viable knockout in organisms that encode TLPs. To determine the function of TLPs in vivo we have generated a viable deletion of a TLP in Mxyococcus xanthus and are characterizing the in vitro activity of MxTLP to obtain insight into potential biological substrates.
Keywords: Thg1, new function, RNA