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Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/17201

Title: Characterization of the Mitochondrial Fusion Protein Mgm1 Reveals Oligomerization and GTPase Activity
Authors: Meglei, Gabriela
Advisor: McQuibban, G. Angus
Department: Biochemistry
Keywords: mitochondrial dynamics
Mgm1
mitochondrial fusion
dynamin
Issue Date: 24-Feb-2009
Abstract: Mitochondrial dynamics resulting from competing fusion and fission reactions are required for normal cellular function in eukaryotes. Mgm1, a dynamin related protein, is a key component in yeast mitochondrial fusion and is evolutionarily conserved. Previous in vivo studies suggest that the GTPase domain and oligomerization are required for Mgm1 mediated mitochondrial inner membrane fusion. This work demonstrates that purified Mgm1 forms dynamic low order oligomers, and has GTPase activity and kinetic properties consistent with a mechanoenzyme and with a role in inner membrane mitochondrial fusion. Mutations of key residues in the GTPase domain show diminished GTPase activity, while a mutation in the GTPase effector domain implicated in self-assembly results in a lower propensity to form oligomers. Together these data indicate that Mgm1 mediates fusion through oligomerization and GTP binding/hydrolysis in a manner similar to other dynamin mechanoenzymes.
URI: http://hdl.handle.net/1807/17201
Appears in Collections:Master
Department of Biochemistry - Master theses

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