The Phosphatase Activities of T4 Polynucleotide Kinase (Rna Ligase, Splicing)

The recent elucidation of the role of the 2':3'-cyclic phosphate in the mechanism of tRNA splicing in wheat germ and yeast prompted a closer examination of the 3'-phosphatase activity of T4 polynucleotide kinase. This resulted in the discovery of not only a 2':3'-cyclic phosphatase activity but also a 2'-phosphatase, in addition to the previously demonstrated 3'-phosphatase. The relationship between the three activities is characterized by determining the pH rate profile, kinetic constants for both ribonucleotide and deoxyribonucleotide substrates and length dependence of each activity. The data suggests that all three activities occur at the same active site. In addition, a model is proposed in which the 2':3'-cyclic phosphatase and kinase activities function with RNA ligase in tRNA breakage and religation.

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

• Weber, Thomas Richard

• Chemistry, Biochemistry

Identifier

(UMI)AAI8511690

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70541