Abstract
Silent information regulator 2 (Sir2) proteins are a class of protein deacetylase enzymes that play key roles in transcriptional gene silencing, DNA repair, and aging. Here, we describe the high-level bacterial expression and purification of a human SirT2 construct that yields high resolution NMR spectra. By removing the N-terminal helix α0 and using Thioredoxin as a fusion partner, greater than 10 mg/L of purified protein can be obtained from minimal media. The protein is fully functional and enables NMR-based screening and structural studies of this important protein.
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