Dynamin Superfamily proteins are involved in the fission and fusion of organelle membranes. One such Dynamin protein, Opa-1, is involved in the fusion of the inner membrane of the mitochondria. More importantly, mutations in this protein have been linked to Dominant Optic Atrophy (DOA), the leading cause of congenital blindness. The Opa-1 protein contains a GTPase region (G-domain) that facilitates the hydrolysis of GTP to dimerize with other Opa-1 proteins. The dimerization of Opa-1 leads to cooperativity that is essential in Opa-1’s function. This research is focusing on the E487K mutation in the G-domain of the Opa-1 protein that has been linked to DOA from previous studies. The goal is to study this mutation’s effect on G-domain dimerization to draw conclusions on the effect of cooperativity and explain the mutation’s link to DOA. Currently, the mutated Opa-1 gene is being cloned in DH5-alpha cells. From there, the mutant protein will be harvested, and the ability of the mutant protein to dimerize will then be compared to the wild-type protein through their initial rates of phosphate production, which will be measured through Colorimetric GTPase Assay with Malachite Green.

In pursuit of the effect of E487K mutation on GTPase domain dimerization of Opa-1 protein

ACS Spring 2022

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