This pore is rimmed with several structurally conserved carbonyl oxygens in addition to the hydroxyl group of the invariant tyrosine from the carboxyl terminus of the SET area (Figure 1 ). Mutation of Tyr245 or Tyr305 in SET7/9 (Determine 4b ) alters its specificity from an H3 K4 mono-methylase to a tri- and solicitor law firm di-methylase, respectively 16 , 21 , whereas an Phe281Tyr mutation within the lysine-binding pocket of DIM-5 (Figure 4c ) converts this protein to an H3 K9 mono- or di-methylase 16 These mutations exemplify the F/Y change (Determine 1 ) that establishes SET-domain product specificities.

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