OBJECTIVE: To obtain the full-length coding sequence of the tree shrew β-amyloid precursor protein cleaving enzyme BACE1 and analyze its molecular characteristics, so as to provide a basis for the research on the mechanism of AD disease.
Methods: The total RNA of tree shrew brain and other organs was extracted, and the sequence obtained by RACE (rapid-amplification of cDNA ends) experiment was spliced with the intermediate sequence to obtain the full-length coding sequence of tree shrew BACE1. DNAMAN、MEGA 10.0.5、 Bioinformatics software such as PyMOL analyzes its sequence and molecular features.
Results: Tree shrew BACE1 was not only expressed in the brain tissue, but also expressed in peripheral tissues. The tree shrew BACE1 nucleic acid sequence and overall protein structure were highly similar to those of humans, and both tree shrew and human BACE1 proteins had a highly conserved intramembrane structure. The ACDL sorting endocytic motif of DXXLL has the same ectodomain, transmembrane domain and intracellular domain, but the tree shrew BACE1 protein has one less potential acetylation site than human, and the folded structure has a difference.
Conclusion: The complete coding sequence of BACE1 gene in tree shrew was obtained in this study, and the basic structure of its protein is basically similar to that of human, suggesting that tree shrew may be an ideal model for studying AD pathological changes or drug research.