Characterization of Molecular Structure-Function Relationships of Escherichia Coli Leucyl-Trna Synthetase

The accurate covalent linkage of amino acid to tRNA for protein synthesis is catalyzed by a family of aminoacyl-tRNA synthetases (aaRS). Some aaRSs have the potential to make mistakes during aminoacylation due to the nature of their amino acid substrate. However, the synthetases have idiosyncratically evolved to include various modules to optimize activity and also enhance fidelity. LeuRS, along with a number of class Ia aaRSs, have acquired a relatively large module called the connective peptide 1 (CP1) domain to correct its mistakes via a hydrolytic amino acid editing mechanism. Surprisingly, deletion of the CP1 domain from Escherichia coli LeuRS yielded a catalytic core that retains fidelity. This suggests that deletion of the CP1 domain may have restored a masked pre-transfer editing mechanism that is inherent in the aminoacylation core.

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

2014

Author dc:creator

• Vu, Michael Tuan

Contributors dc:contributor

• Martinis, Susan A.

• Chemistry, Biochemistry

Identifier

(UMI)AAI3314928

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/72335