Probing the Role of Highly Conserved Lysine (K279) Residue in the Editing Domain of Bacterial Prolyl-tRNA Synthetases
File(s)
Date
2011-05Author
Mueller, Irene C.
Cao, Bach
Meitzner, Karl J.
Tschudy, Matthew J.
Advisor(s)
Bhattacharyya, Sudeep
Hati, Sanchita
Metadata
Show full item recordAbstract
The Escherichia coli (Ec) prolyl-tRNA synthetase enzyme possesses three distinct domains. One of the domains, the editing domain, is critical for proofreading the charged tRNAPro, ensuring the correct amino acid has been attached to the tRNA
molecule. In this editing domain, a highly conserved lysine has been found to be absolutely essential for proofreading. Through site-directed mutagenesis and enzyme kinetic studies this study attempted to probe the role of this lysine residue (K279).
Subject
Catalytic RNA
Functional analysis
Escherichia coli
Lysine
Posters
Ligases
Microbiological synthesis
Permanent Link
http://digital.library.wisc.edu/1793/55083Description
Color poster with text, diagrams, charts, and graphs.