Our laboratory is working on identifying proteins that are palmitoylated by a nonenzymatic mechanism in vivo.  Addition of palmitate to proteins facilitates their membrane interactions and trafficking, and it modulates protein-protein interactions and enzyme activity.  We have adapted a fatty acid exchange protocol by using benzyloxybenzylbromide resins to purify and isolate palmitoylated proteins from obese Zucker rat tissue.  We were able to successfully identify several putatively palmitoylated proteins using mass spectrometric techniques.  Mass spectral analysis of in vitro palmitoylated catalase enzyme revealed that a peptide with the sequence RLC*ENIAGHLK contained a palmitoylated cysteine residue.  This cysteine is situated close to the entrance channel used by H2O2 to access the deeply buried heme group and is conserved throughout all catalases from all species.  The palmitoylation of this cysteine may result in a membrane-bound form of the catalase enzyme that has the active site oriented towards the membrane surface.

Isolation of palmitoylated proteins from obese Zucker rats

244th National Meeting (2012)

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