This pore is rimmed with a number of structurally conserved carbonyl oxygens as well as the hydroxyl group of the invariant tyrosine from the carboxyl terminus of the SET domain (Figure 1 ).

Taipale M, Rea S, Richter Okay, Vilar A, Lichter P, Imhof A, Akhtar A: hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells. Mutation of Tyr245 or Tyr305 in SET7/9 (Figure 4b ) alters its specificity from an H3 K4 mono-methylase to a tri- and di-methylase, respectively sixteen , 21 , whereas an Phe281Tyr mutation in the lysine-binding pocket of DIM-5 (Determine 4c ) converts this protein to an H3 K9 mono- or di-methylase 16 These mutations exemplify the F/Y switch (Determine 1 ) that establishes SET-area product specificities.

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