AI Article Synopsis
- SIRT6 is a histone deacetylase that modifies proteins but has low activity in lab settings.
- The study presents a method to track how SIRT6 deacetylates a specific protein, long-chain acyl-CoA synthase 5, when palmitic acid is present.
- The protocol includes steps for purifying SIRT6 and its substrate, as well as a deacetylation assay that can be applied to various research scenarios involving SIRT6.
Article Abstract
The histone deacetylase known as sirtuin 6 (SIRT6) deacetylates both histone and non-histone proteins but has low deacetylase activity in vitro. Here, we present a protocol to monitor SIRT6-mediated deacetylation of long-chain acyl-CoA synthase 5 in the presence of palmitic acid. We describe the purification of His-SIRT6 and a Flag-tagged substrate. We then detail a deacetylation assay protocol that can be widely applied to study other SIRT6-mediated deacetylation events and the effect of SIRT6 mutations on its activity. For complete details on the use and execution of this protocol, please refer to Hou et al. (2022)..
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10090442 | PMC |
| http://dx.doi.org/10.1016/j.xpro.2023.102206 | DOI Listing |
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