화학공학소재연구정보센터
Applied Biochemistry and Biotechnology, Vol.177, No.4, 957-966, 2015
Human and Tree Shrew Alpha-synuclein: Comparative cDNA Sequence and Protein Structure Analysis
The synaptic protein alpha-synuclein (alpha-syn) is associated with a number of neurodegenerative diseases, and homology analyses among many species have been reported. Nevertheless, little is known about the cDNA sequence and protein structure of alpha-syn in tree shrews, and this information might contribute to our understanding of its role in both health and disease. We designed primers to the human alpha-syn cDNA sequence; then, tree shrew alpha-syn cDNA was obtained by RT-PCR and sequenced. Based on the acquired tree shrew alpha-syn cDNA sequence, both the amino acid sequence and the spatial structure of alpha-syn were predicted and analyzed. The homology analysis results showed that the tree shrew cDNA sequence matches the human cDNA sequence exactly except at nucleotide positions 45, 60, 65, 69, 93, 114, 147, 150, 157, 204, 252, 270, 284, 298, 308, and 324. Further protein sequence analysis revealed that the tree shrew alpha-syn protein sequence is 97.1 % identical to that of human alpha-syn. The secondary protein structure of tree shrew alpha-syn based on random coils and alpha-helices is the same as that of the human structure. The phosphorylation sites are highly conserved, except the site at position 103 of tree shrew alpha-syn. The predicted spatial structure of tree shrew alpha-syn is identical to that of human alpha-syn. Thus, alpha-syn might have a similar function in tree shrew and in human, and tree shrew might be a potential animal model for studying the pathogenesis of alpha-synucleinopathies.