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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 16 , 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-domain product specificities.

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Min J, Zhang X, Cheng X, Grewal SI, Xu RM: Structure of the SET domain histone lysine methyltransferase Clr4.

On the base of the channel is the methyltransfer pore, which connects the pocket to the AdoMet-binding cleft. The exception to the rule is the DOT1 family, members of which methylate K79 in the globular region of histone H3 and which are structurally not associated to SET-area proteins four - 6 Latest work means that SET-area-containing proteins methylate a few proteins along with histones (see later)