BIOCHEMICAL ANALYSIS OF TWO DISTINCT METHIONYL-TRNA SYNTHETASES

Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that catalyze the attachment of amino acids to their cognate tRNAs for protein biosynthesis at the ribosome. The long term objective of this project is to investigate catalytic features of methionyl-tRNA synthetase (MetRS) from two different organisms. MetRS is proposed to use long-range communication between its anticodon binding and catalytic active sites. MetRS also exhibits structural variability in different organisms including different oligomeric states and appended domains. In this dissertation, our goal was to understand how long-range communication occurs in E. coli MetRS and what additional functions are contributed by the large appended domain of M. penetrans MetRS.

Grantor dc:publisher

Wake Forest University

Year dc:date.issued

2014

Author dc:creator

• Sharma, Sandhya Bharti

• Aminotransferase

Language dc:language.iso

en

Handle dc:identifier.uri

http://hdl.handle.net/10339/47452

OAI identifier oai:identifier

oai:wakespace.lib.wfu.edu:10339/47452