Date of Award
2006
Degree Type
Thesis
Degree Name
Master of Science
Program
Biochemistry
Supervisor
Dr. David Haniford
Second Advisor
Dr Megan Davey
Third Advisor
Dr. David Litchfield
Abstract
H-NS enhances TnlO transposition by directly binding to the transposition complex (transpososome) and unfolding it. In an unfolded state, inteπnolecular transposition events are favored. The purpose of this study was to further understand what functions of H-NS are required for the formation of a stably unfolded transpososome. To determine what functions of H-NS are essential, specific H-NS mutants were generated and tested for their abilities to stimulate transposition in vitro and interact with the transpososome. Four major conclusions regarding H-NS interaction with the Tnlθ transpososome were drawn. First, H-NS initially binds the transpososome through DNA structure specific recognition. Secondly, upon unfolding of the transpososome, H-NS makes a direct protein-protein interaction with transposase. Thirdly, H-NS alters the IHF binding site to potentially prevent IHF from refolding the transpososome. Finally, H-NS is able to influence target site selection in TnlO transposition.
Recommended Citation
Ward, Chris, "MECHANISMS FOR H-NS ACTION IN Tnl0 TRANSPOSITION" (2006). Digitized Theses. 4985.
https://ir.lib.uwo.ca/digitizedtheses/4985