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oai:www.ideals.illinois.edu:2142/70541 2023-07-11 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

Weber, Thomas Richard 2014-12-15T23:43:51Z 2014-12-15T23:43:51Z 10000-01-01 1985 1985 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. Made available in DSpace on 2014-12-15T23:43:51Z (GMT). No. of bitstreams: 1 8511690.pdf: 3368765 bytes, checksum: 680a683534c2fb9b8410b78ed09e09ab (MD5) Previous issue date: 1985 Embargo set by: Seth Robbins for item 70707 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 116 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1985. http://hdl.handle.net/2142/70541 (UMI)AAI8511690 Chemistry, Biochemistry The Phosphatase Activities of T4 Polynucleotide Kinase (Rna Ligase, Splicing) text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.