SUMMARY

Parkinson’s Disease (PD), a neurodegenerative disease, is the most common movement disorder in which dopaminergic neurons die. Some apparent symptoms of PD include tremors, muscle rigidity, and changes in speech. A protein that is neuropathologically linked to PD is ⍺-synuclein. It is of great interest to study ⍺-synuclein since its misfolding and formation of Lewy bodies have causational effects on PD. However, the extent to which ⍺-synuclein is involved in all cases of PD still remains unclear. For our research, we used yeast (Saccharomyces cerevisiae) which is a common model organism used to study PD. We hypothesized that truncating ⍺-synuclein to amino acid fragments 1-65 and 1-125 will cause a mutation that will promote an increase in aggregation. We successfully truncated the C terminus of ⍺-synuclein by PCR and gene purification. Then, we sub-cloned the fragments into the pYES2 vector, performed bacterial transformation, and checked the fragments for correct gene orientation. Following conformation of our sequences, we transformed the fragments into yeast. Our project plays a significant role in prepping for further research to test the importance of the C terminus in ⍺-synuclein and its effects on PD. 

By studying different domains of ⍺-synuclein, it could allow for valuable research to investigate effects of mutated ⍺-synuclein in PD. 

(Note from web manager: due to technical difficulties, this article will only be available in PDF form)

Related Links:

• 16_44 Cosmo et al. (PDF)