2K3X: Solution structure of EAF3 chromo barrel domain

Deacetylation of nucleosomes by the Rpd3S histone deacetylase along the path of transcribing RNA polymerase II regulates access to DNA, contributing to faithful gene transcription. The association of Rpd3S with chromatin requires its Eaf3 subunit, which binds histone H3 methylated at lysine 36 (H3K36). Eaf3 is also part of NuA4 acetyltransferase that recognizes methylated H3K4. Here we show that Eaf3 in Saccharomyces cerevisiae contains a chromo barrel-related domain that binds methylated peptides, including H3K36 and H3K4, with low specificity and millimolar-range affinity. Nuclear magnetic resonance structure determination of Eaf3 bound to methylated H3K36 was accomplished by engineering a linked Eaf3-H3K36 molecule with a chemically incorporated methyllysine analog. Our study uncovers the molecular details of Eaf3-methylated H3K36 complex formation, and suggests that, in the cell, Eaf3 can only function within a framework of combinatorial interactions. This work also provides a general method for structure determination of low-affinity protein complexes implicated in methyllysine recognition.
PDB ID: 2K3XDownload
MMDB ID: 66673
PDB Deposition Date: 2008/5/19
Updated in MMDB: 2008/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 2K3X
Label Count Molecule
Protein (1 molecule)
Chromatin Modification-related Protein Eaf3(Gene symbol: EAF3)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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