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Title page for ETD etd-08242011-132833


Type of Document Dissertation
Author Bairley, Robin Christine Brooks
URN etd-08242011-132833
Title Contributions to telomerase anchor-site and template/primer alignment functions by yeast TERT residue E76
Degree PhD
Department Biological Sciences
Advisory Committee
Advisor Name Title
Todd Graham Committee Chair
Carl Johnson Committee Member
David Cortez Committee Member
Katherine Friedman Committee Member
Kathy Gould Committee Member
Keywords
  • Telosome
  • Processivity
  • TLC1
Date of Defense 2011-08-18
Availability unrestricted
Abstract
This project explores the synthesis of heterogeneous G1-3T yeast telomere sequences by the enzyme telomerase. I demonstrate that a mutant in the essential N-terminal TEN domain of Est2p (telomerase reverse transciptase), glutamic acid 76 to lysine (est2-LTE76K), restricted possible alignments between the DNA primer and the RNA template and increased in vivo processivity. Within the context of telomerase, the Est2p TEN domain is thought to contribute to enzyme processivity by mediating an anchor-site interaction with the DNA primer. I showed that binding of the purified TEN domain (residues 1-161) to telomeric DNA is enhanced by the E76K mutation. These results suggest a novel role for the anchor-site in mediating primer/template alignment within the active site of yeast telomerase.
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