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. Author manuscript; available in PMC: 2010 Dec 1.
Published in final edited form as: FEBS J. 2009 Nov 6;276(23):7159–7176. doi: 10.1111/j.1742-4658.2009.07427.x

Figure 1.

Figure 1

TbSIR2 ADP-ribosylates unacetylated H1.1.

(A) Autoradiograph of the enzyme-dependent ADP-ribosylation of unacetylated H1.1. Reactions were carried out using wild type TbSIR2. The catalytic mutants were used as control reactions. (B) 32P-incorporation into unacetylated H1.1 was determined for wild type TbSIR2 and the catalytic mutant TbH142Y. (C) TbSIR2 ADP-ribosylation of unacetylated H1.1 displays concentration dependent inhibition with nicotinamide. (D) Phosphodiesterase treatment removes the radiolabel from unacetylated H1.1 treated with TbSIR2 and 32P-NAD+. (E) Autoradiograph of ADP-ribosylation reactions using acetylated and unacetylated histone H1.1 as substrates.