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Is Arabidopsis thaliana gamma‐secretase a functional protease? (934.7)
Author(s) -
Lee Jamie,
Dries Daniel
Publication year - 2014
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.28.1_supplement.934.7
Subject(s) - nicastrin , presenilin , gamma secretase , arabidopsis thaliana , arabidopsis , alpha secretase , biology , microbiology and biotechnology , recombinant dna , amyloid precursor protein , chemistry , biochemistry , alzheimer's disease , gene , mutant , disease , medicine , pathology
gamma‐secretase is a multisubunit proteolytic complex responsible for the final step of the formation of beta‐amyloid peptides. Neurotoxic beta‐amyloid peptides are the primary components of amyloid plaques that, along with neurofibrillary tangles of tau protein, are found in the brains of Alzheimer’s disease patients. The gamma‐secretase complex contains four proteins _ presenilin, nicastrin, Aph‐1, and Pen‐2 _ and the presence of all four components is required for proteolytic activity of the complex. Surprisingly, all four proteins co‐evolved in plants, suggesting that a shared function was also conserved. However, since plants do not have nervous system, nor do they suffer from Alzheimer's disease, the function of plant gamma‐secretase is still a mystery. In this study, we subclone four components of Arabidopsis thaliana gamma‐secretase into a single plasmid in order to generate recombinant baculovirus for expression of Arabidopsis gamma‐secretase in Sf9 host cells. This allows for the simultaneous recombinant expression of four proteins in the same cell and from a single plasmid, thereby ensuring 100% co‐infection by all four gamma‐secretase components. This, then, gives us a powerful tool to study the putative proteolytic function of recombinant Arabidopsis gamma‐secretase in vitro.