The proposed research focuses on examining a transcription termination system in Gram positive bacteria. This system uses an RNA to control gene expression by binding lysine. Conserved sequence and structural patters has identified a number of genes within the lysine biosynthetic pathway that contain features characteristic of transcription termination systems. These features include competing terminator and anti-terminator structures. Studies done by the Henkin lab have shown that the lysC leader RNA has the ability to directly bind lysine at physiological concentrations (3mM), while discriminating against other products of the pathway. This specificity and high affinity for lysine warrants the investigation of the molecular mechanism of ligand binding. Our approach to understanding the system involves the characterization of mutants with an altered affinity for lysine and lysine analogs. With this work we hope to identify particular residues and contacts important for ligand binding .

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Predoctoral Individual National Research Service Award (F31)
Project #
7F31GM076894-05
Application #
7749937
Study Section
Minority Programs Review Committee (MPRC)
Program Officer
Toliver, Adolphus
Project Start
2006-01-03
Project End
2011-01-02
Budget Start
2010-01-03
Budget End
2011-01-02
Support Year
5
Fiscal Year
2010
Total Cost
$33,196
Indirect Cost
Name
Ohio State University
Department
Microbiology/Immun/Virology
Type
Schools of Arts and Sciences
DUNS #
832127323
City
Columbus
State
OH
Country
United States
Zip Code
43210
Wilson-Mitchell, Sharnise N; Grundy, Frank J; Henkin, Tina M (2012) Analysis of lysine recognition and specificity of the Bacillus subtilis L box riboswitch. Nucleic Acids Res 40:5706-17
Ataide, Sandro F; Wilson, Sharnise N; Dang, Sandy et al. (2007) Mechanisms of resistance to an amino acid antibiotic that targets translation. ACS Chem Biol 2:819-27