2K3X

Solution structure of EAF3 chromo barrel domain

2K3X の概要

• エントリーDOI: 10.2210/pdb2k3x/pdb
• 分子名称: Chromatin modification-related protein EAF3 (1 entity in total)
• 機能のキーワード: eaf3, chromo barrel domain, histone deacetylase, methylated histones h3k36 and h3k4, chromatin regulator, dna damage, dna repair, nucleus, phosphoprotein, transcription, transcription regulation, transcription regulator
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Nucleus: Q12432
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14103.97

構造登録者

Mer, G.,Xu, C. (登録日: 2008-05-19, 公開日: 2008-09-16, 最終更新日: 2024-05-29)

主引用文献

Xu, C.,Cui, G.,Botuyan, M.V.,Mer, G.
Structural Basis for the Recognition of Methylated Histone H3K36 by the Eaf3 Subunit of Histone Deacetylase Complex Rpd3S.
Structure, 16:1740-1750, 2008

PubMed Abstract: 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.

PubMed: 18818090
DOI: 10.1016/j.str.2008.08.008

実験手法

SOLUTION NMR