Talk abstracts

Talk on Saturday 10:20-10:40am submitted by John Means

Structural studies of the Bacillus subtilis T box antiterminator/tRNA model complex

John A. Means (Chemistry and Biochemistry, Ohio University), Crystal M. Simson (Chemistry and Biochemistry, Ohio University), Jeffrey J. Rack (Chemistry and Biochemistry, Ohio University), Jennifer V. Hines (Chemistry and Biochemistry, Ohio University)

Abstract:
The T box antitermination system, which is located in the mRNA 5' untranslated leader region, is a tRNA-sensing riboswitch that exerts transcriptional control over many Gram-positive bacterial tRNA synthetase, amino acid biosynthesis, and amino acid transport genes (1). Control depends on the stabilization of a highly-conserved antiterminator structure via the binding of the gene's uncharged cognate tRNA (2). If the antiterminator is not stabilized, a competing terminator structure forms, halting transcription (3). The current investigations revolve around the structural features involved in the recognition of the tRNA acceptor stem by the antiterminator. Structural changes that occur in the antiterminator upon its binding with a microhelix tRNA model have been studied, allowing the derivation of a model for the binding of these two RNAs.

References:
1. Grundy, F. J. and Henkin, T. M. Crit. Rev. Biochem. Mol. Biol. 2006, 41, 329-338.
2. Grundy, F. J., et al. Nucleic Acids Res. 2002, 30, 1646-1655.
3. Grundy, F. J., et al. RNA, 2000, 30, 1065-1072.

Keywords: mRNA−tRNA interaction, riboswitch, fluorescence