Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor

Joseph Lee, James R. Thompson, Maria Victoria Botuyan, Georges Mer

Research output: Contribution to journalArticle

145 Scopus citations

Abstract

The lysine demethylase JMJD2A has the unique property of binding trimethylated peptides from two different histone sequences (H3K4me3 and H4K20me3) through its tudor domains. Here we show using X-ray crystallography and calorimetry that H3K4me3 and H4K20me3, which are recognized with similar affinities by JMJD2A, adopt radically different binding modes, to the extent that we were able to design single point mutations in JMJD2A that inhibited the recognition of H3K4me3 but not H4K20me3 and vice versa.

Original languageEnglish (US)
Pages (from-to)109-111
Number of pages3
JournalNature Structural and Molecular Biology
Volume15
Issue number1
DOIs
StatePublished - Jan 1 2008

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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