Abstract
The most common form of familial amyloid polyneuropathy (FAP) is caused by the transthyretin (TTR) methionine 30 (Met30) mutation. However, the mechanisms of TTR-amyloid fibril formation remain poorly understood. We established a genetic assay based on the yeast two-hybrid system to study TTR inter-molecular interactions. Two functional domains of the GAL4 transcriptional activator were cloned into two different expression vectors. TTR monomeric sequences were fused with either of these two domains and co-expressed in yeast. An intense inter-molecular binding between wild-type TTR monomers was detected in the yeast, as indicated by the expression of β-galactosidase activity. When one of the wild-type TTR was replaced with Met30 mutant TTR, the β-galactosidase activity was reduced by more than 57%. When both fusion proteins contained Met30 mutant, the β-galactosidase activity was reduced by 84%. This result suggests that the presence of Met30 mutation markedly reduces TTR inter-molecular interaction in thi...
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