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Expression of Microtubule Associated Protein Tau (MAPT) in Saccharomyces cerevisiae to Determine the Effects of N‐terminal Acetylation
Author(s) -
Anderson Jess Lynn,
Holmes William
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.464.1
Subject(s) - acetylation , microtubule , yeast , tau protein , proteome , saccharomyces cerevisiae , biochemistry , phenotype , biology , acetyltransferase , chemistry , microbiology and biotechnology , gene , medicine , disease , pathology , alzheimer's disease
Protein aggregates, which can result in cellular toxicity, are found in the brains of people afflicted with neurodegenerative diseases. One of the proteins found to aggregate is the Microtubule Associated Protein Tau, a protein that stabilizes microtubules in neuronal cells. Based on its amino acid sequence, Tau is predicted to be N‐terminally acetylated by the acetyltransferase complex NatA, which is responsible for the acetylation of 50% of the proteome in yeast and humans. Loss of NatA activity results in a variety of pleiotropic detrimental phenotypes, suggesting that acetylation is a crucial modification for many proteins. The first 10 amino acids of Tau have previously been demonstrated to play a role in aggregation, but the specific role of N‐terminal acetylation has yet to be determined. Without the presence of NatA – and therefore without acetylation – Tau may be more prone to aggregation and toxicity. By expressing Tau in yeast strains with and without the presence of NatA, the possible effects of acetylation or lack thereof can be determined by examining protein expression and aggregation within the cells by various methods including SDS‐PAGE, SDD‐AGE, and visualization of GFP‐tagged Tau via microscopy. Support or Funding Information This work was made possible by an Early Career Development Award through RI‐INBRE (2P20GM103430) and by Dr. William Holmes. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .