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Determining the role of protein regulators of hisactophilin on actin filament formation

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Title: Determining the role of protein regulators of hisactophilin on actin filament formation
Author: McRorie, Paul Alexander
Department: Department of Molecular and Cellular Biology
Program: Biophysics
Advisor: Dawson, John
Abstract: Protein structure and functions are tightly regulated. Studying the integration of multiple modifications in single systems is a novel approach. Hisactophilin protein from Dictyostelium discoideum, is an actin binding protein that serves to induce formation of actin filaments and is regulated by protonation and myristoylation. Utilizing hisactophilin as a model, I determined the effect of pH and myristoyl-switching on actin binding and filament induction using fluorescence spectroscopy, light scattering, and time-course electron microscopy. Results revealed the accessible myristoyl group slows binding and the rate of actin polymerization compared to when the group is sequestered. Hisactophilin induces pH-dependent actin aggregates before reorganizing them into filaments and bundles. Hisactophilin mutants impact initial actin binding and the kinetics of the aggregated state. I determined the cooperativity of myristoylation and protonation as interdependent protein regulatory mechanisms, their impact on actin binding and proposed a novel mechanism for actin polymerization as a result of these integrated regulators.
URI: http://hdl.handle.net/10214/5264
Date: 2012-12
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http://creativecommons.org/licenses/by/2.5/ca/ Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by/2.5/ca/