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For instance, human SET7/9 has recently been reported to methylate Lys189 within the general transcription factor TAF10, leading to an elevated affinity for RNA polymerase II and transcriptional activation of sure TAF10-dependent genes 37 SET7/9 has additionally been reported to methylate p53, rising the stability of this short lived tumor-suppressor protein 38 These observations counsel that we should not narrowly outline the SET-area proteins as histone lysine methyltransferases but as an alternative call them protein lysine methyltransferases.
This pore is rimmed with several structurally conserved carbonyl oxygens as well as the hydroxyl group of the invariant tyrosine from the carboxyl terminus of the SET domain (Figure 1 ). These carbonyl and hydroxyl oxygens have been proposed to facilitate the transfer of the methyl group throughout catalysis sixteen , 21 , solicitor law firm 24 As well as, tyrosine residues within the lysine-binding clefts of SET7/9 (Tyr245 and Tyr305) and DIM-5 (Tyr178) hydrogen-bond to the lysine ε-amino group, aligning it for a methyltransfer with AdoMet (Determine 4b,c ). 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 sixteen These mutations exemplify the F/Y change (Figure 1 ) that establishes SET-area product specificities.
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Ini akan menghapus halaman "Clinical Proteomics"
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