Synuclein Proteins of the Pufferfish Fugu rubripes: Sequences and Functional Characterization

Yoshida, Hirotaka, Craxton, Molly, Jakes, Ross, Zibaee, Shahin, Tavare, Richard, Fraser, Graham, Serpell, Louise, Davletov, Bazbek, Crowther, R. Anthony and Goedert, Michel (2006) Synuclein Proteins of the Pufferfish Fugu rubripes: Sequences and Functional Characterization. Biochemistry, 45 (8). pp. 2599-2607. ISSN 0006-2960

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Abstract

In humans, three genes encode the related a-, ß-, and ¿-synucleins, which function as lipid-binding proteins in vitro. They are being widely studied, mainly because of the central involvement of a-synuclein in a number of neurodegenerative diseases, including Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. In these diseases, the normally soluble a-synuclein assembles into abnormal filaments. Here, we have identified and characterized the synuclein gene family from the pufferfish Fugu rubripes. It consists of four genes, which encode a-, ß-, ¿1-, and ¿2-synucleins. They range from 113 to 127 amino acids in length and share many of the characteristics of human synucleins, including the presence of imperfect amino-terminal repeats of 11 amino acids, a hydrophobic middle region, and a negatively charged carboxy-terminus. All four synucleins are expressed in the Fugu brain. Recombinant Fugu synucleins exhibited differential liposome binding, which was strongest for a-synuclein, followed by ß-, ¿2-, and ¿1-synucleins. In assembly experiments, Fugu a-, ¿1-, and ¿2-synucleins formed filaments more readily than human a-synuclein. Fugu ß-synuclein, by contrast, failed to assemble in bulk. Filament assembly of synucleins was directly proportional to their degree of hydrophobicity and their tendency to form ß-sheet structure, and correlated inversely with their net charge.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Louise Serpell
Date Deposited: 06 Feb 2012 18:22
Last Modified: 19 Mar 2012 14:10
URI: http://sro.sussex.ac.uk/id/eprint/16025
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