Abstract
Mutations in OPA1 are associated with DOA or DOA plus. Novel mutations in OPA1 are periodically identified, but often the causative effect of the mutation is not demonstrated. A chimeric protein containing the N-terminal region of Mgm1, the yeast orthologue of OPA1, and the C-terminal region of OPA1 was constructed. This chimeric construct can be exploited to evaluate the pathogenicity of most of the missense mutations in OPA1 as well as to determine whether the dominance of the mutation is due to haploinsufficiency or to gain of function.
Keywords:
DOA; DOA plus; MGM1/OPA1 chimeric constructs; Modeling human mutations; Yeast model.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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DNA Mutational Analysis*
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GTP Phosphohydrolases / genetics*
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GTP Phosphohydrolases / metabolism*
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GTP-Binding Proteins / genetics*
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GTP-Binding Proteins / metabolism*
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Humans
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Mitochondrial Proteins / genetics*
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Mitochondrial Proteins / metabolism*
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Mutation, Missense
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Optic Atrophy, Autosomal Dominant / genetics*
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae Proteins / genetics*
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Saccharomyces cerevisiae Proteins / metabolism*
Substances
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MGM1 protein, S cerevisiae
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Mitochondrial Proteins
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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GTP Phosphohydrolases
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GTP-Binding Proteins
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OPA1 protein, human