Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay.
Synphilin-1 interacts with alpha-synuclein, which has been implicated in the pathogenesis of Parkinson's disease (PD). By examination of their interactions quantitatively, with the use of the yeast two-hybrid beta-galactosidase assay, we find that the synuclein amino acid (aa) 1-65 region is sufficient for an interaction. A central domain of synphilin-1, ... aa 349-555, is both necessary and sufficient for an interaction with alpha-synuclein. We did not observe an effect of the synuclein A53T mutation, which causes one familial form of PD, on interactions with synphilin-1. However, the A30P mutation caused an increase in the interaction between the synuclein aa 1-65 fragment and the synphilin-1 central domain.
Mesh Terms:
Carrier Proteins, Drug Interactions, Humans, Mutation, Nerve Tissue Proteins, Protein Isoforms, Synucleins, Two-Hybrid System Techniques, alpha-Synuclein, beta-Galactosidase
Carrier Proteins, Drug Interactions, Humans, Mutation, Nerve Tissue Proteins, Protein Isoforms, Synucleins, Two-Hybrid System Techniques, alpha-Synuclein, beta-Galactosidase
Neurosci. Lett.
Date: Jun. 07, 2002
PubMed ID: 12044636
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