Characterization of Leucyl -Trna Synthetase From Escherichia Coli and Saccharomyces Cerevisiae in Aminoacylation, Amino Acid Editing, and Protein-Dependent RNA Splicing

Using extensive deletion and site-directed mutagenesis, we characterized the C-terminal domain of LeuRSs from different origins to understand its role. The results demonstrated that the native environment of the enzyme influenced the functional role of the unique C-terminal domain of both LeuRSs. These combined biochemical investigations suggest that the yeast mitochondrial LeuRS C-terminal domain has uniquely adapted to accommodate aminoacylation, amino acid editing, and RNA-protein interactions.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Hsu, Jennifer Ling

Contributors dc:contributor

• Susan Martinis

• Chemistry, Biochemistry

Language dc:language

eng

Identifier

(MiAaPQ)AAI3250259

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84835