Role of Coupled Domain Motions on the Catalytic Activity of Escherichia coli Prolyl-tRNA Synthetase.
Date
2009-04Author
Cao, Bach
Greene, Alexander J.
Zimmerman, Kurt A.
Advisor(s)
Hati, Sanchita
Metadata
Show full item recordAbstract
Prolyl-tRNA synthetases (ProRSs), which are class II synthetases that catalyze covalent attachment of proline to the 3'end of the tRNAPro. ProRSs from all three kingdoms of life, have shown to misactivate noncognate alanine and cysteine, and
form mischarged aminoacyl?tRNAPro. It has been found that the insertion domain (?180 amino acids) of Escherichia coli (Ec) ProRS is the post-transfer editing active site that hydrolyzes specifically mischarged alanyl-tRNAPro. Herein, we report the effect of mutations on highly conserved residues (G217 and E218) located on the loop
connecting the catalytic and editing domains of Ec ProRS.
Subject
Posters
Catalytic RNA
Escherichia coli
Ligases
Permanent Link
http://digital.library.wisc.edu/1793/36123Description
Color poster with text, images, chart and diagrams.