Skip to main content
. Author manuscript; available in PMC: 2010 Apr 6.
Published in final edited form as: Nat Struct Mol Biol. 2009 Dec 20;17(1):38–43. doi: 10.1038/nsmb.1753

Figure 3.

Figure 3

Effect of the linker on the KIAA1718 jumonji activity targeting H3K9me2. (a) ITC measurements of binding of the KIAA1718 to doubly methylated H31–24K4me3-K9me2 peptides (left) and H31–24K9me2 peptides (right). The measurements were carried out under the conditions of 18 µM protein concentration and 0.4 mM peptide concentration in 50 mM NaCl and 50 mM HEPES, pH 7.0. (b) Superimposition of PHF8 (colored) and KIAA1718 (gray) in their respective jumonji domains. (c) The engineered hybrid enzyme of KIAA1718 carrying the PHF8 linker gains substantial activity on H31–24K3me3-K9me2 (right), faster by a factor of more than 100 than that of the wild-type enzyme (see Fig. 2a).