Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal

TLDR

The authors isolated a 143‑amino‑acid neuron‑specific protein, synuclein, by using an antiserum against Torpedo cholinergic synaptic vesicles and expression screening, and also identified a highly homologous 140‑amino‑acid clone from a rat brain cDNA library. Synuclein’s N‑terminal 100 residues contain an 11‑residue repeat with a conserved core, the gene is expressed exclusively in nervous tissue, and the protein exists in 17.5, 18.5, and 20.0 kDa forms in Torpedo synapses, with the 17.5‑kDa species predominating in neuronal soma and localizing to the nuclear envelope.

Abstract

We used an antiserum against purified cholinergic synaptic vesicles from Torpedo and expression screening to isolate a cDNA clone encoding synuclein, a 143 amino acid neuron-specific protein. A cDNA clone was also isolated from a rat brain cDNA library that encodes a highly homologous 140 amino acid protein. The amino terminal 100 amino acids of both proteins are comprised of an 11 amino acid repeating unit that contains a conserved core of 6 residues. The synuclein gene is expressed only in nervous system tissue, not in electric organ, muscle, liver, spleen, heart, or kidney. In the electric organ synapse Torpedo synuclein-immunoreactive proteins are found in 3 major molecular-weight classes of 17.5, 18.5, and 20.0 kDa. In the neuronal cell soma the 17.5 kDa species is predominant and immunoreactivity is localized to a portion of the nuclear envelope.