Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3

We have focused on elucidating the speci®city of methyl-K9 recognition using a series of H3 tail peptides described in Materials and methods

Steven A. Jacobs; Sean D. Taverna; Yinong Zhang; Scott D. Briggs; Jinmei Li; Joel C. Eissenberg; C. David Allis; Sepideh Khorasanizadeh

2002

Scholarcy highlights

  • Using an antibody speci®c for methyl-K9 H3, we show that this methylationhistone code' and HP1 protein co-localize in situ on Drosophila polytene chromosome squashes
  • We show that the chromo domain of Esa1 histone acetyltransferase does not interact with the methyl-K9 H3 tail, but it has avidity for the unmodi®ed H3 tail
  • Using isothermal titration calorimetry, we have obtained additional thermodynamic parameters that characterize the interaction of the chromo domain with methyl-K9 H3 tail
  • We demonstrate, using a methyl-K9 H3-speci®c antibody, that this methylation mark and HP1 protein co-localize in situ on Drosophila polytene chromosome squashes
  • H3 peptide binding that are not detected with either unmodi®ed or methyl-K4 H3 peptides. These perturbations occur in the chromo domain of HP1 and suggest a high degree of selectivity in binding of methylated peptide. This property of HP1 may play an important role in recognizing methyl-K9 for theoff' state of transcription in heterochromatin, distinguishing it from methyl-K4, which has been associated with theon' state of transcription
  • Thermodynamic parameters for methyl-K9 H3 peptide binding to the chromo domain were determined by standard isothermal titration calorimetry methods conducted at

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