Molecular recognition of histone lysine methylation by the Polycomb group repressor dSfmbt

  • Grimm C
  • Matos R
  • Ly-Hartig N
 et al. 
  • 58

    Readers

    Mendeley users who have this article in their library.
  • 57

    Citations

    Citations of this article.

Abstract

Polycomb group (PcG) proteins repress transcription by modifying chromatin structure in target genes. dSfmbt is a subunit of the Drosophila melanogaster PcG protein complex PhoRC and contains four malignant brain tumour (MBT) repeats involved in the recognition of various mono- and dimethylated histone peptides. Here, we present the crystal structure of the four-MBT-repeat domain of dSfmbt in complex with a mono-methylated histone H4 peptide. Only a single histone peptide binds to the four-MBT-repeat domain. Mutational analyses show high-affinity binding with low peptide sequence selectivity through combinatorial interaction of the methyl-lysine with an aromatic cage and positively charged flanking residues with the surrounding negatively charged surface of the fourth MBT repeat. dSfmbt directly interacts with the PcG protein Scm, a related MBT-repeat protein with similar methyl-lysine binding activity. dSfmbt and Scm co-occupy Polycomb response elements of target genes in Drosophila and they strongly synergize in the repression of these target genes, suggesting that the combined action of these two MBT proteins is crucial for Polycomb silencing.

Author-supplied keywords

  • Histone modifications
  • MBT repeat
  • Methyl-lysine recognition
  • Polycomb group proteins

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Clemens Grimm

  • Raquel Matos

  • Nga Ly-Hartig

  • Ulrich Steuerwald

  • Doris Lindner

  • Vladimir Rybin

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free