6J2P

Crystal structure of Saccharomyces cerevisiae Spp1 in complex with H3K4me3

6J2P の概要

• エントリーDOI: 10.2210/pdb6j2p/pdb
• 分子名称: COMPASS component SPP1, Histone H3, ZINC ION (3 entities in total)
• 機能のキーワード: histone modification recognition, protein binding
• 由来する生物種: Saccharomyces cerevisiae S288c (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 61045.54

構造登録者

He, C.,Li, F. (登録日: 2019-01-02, 公開日: 2019-09-11)

主引用文献

He, C.,Liu, N.,Xie, D.,Liu, Y.,Xiao, Y.,Li, F.
Structural basis for histone H3K4me3 recognition by the N-terminal domain of the PHD finger protein Spp1.
Biochem.J., 476:1957-1973, 2019

PubMed Abstract: Spp1, a plant homeodomain (PHD) finger containing protein, is a critical subunit of the histone H3K4 methyltransferase complex of proteins associated with Set1 (COMPASS). The chromatin binding affinity of the PHD finger of Spp1 has been proposed to modulate COMPASS activity. During meiosis, Spp1 plays another role in promoting programmed double-strand break (DSB) formation by binding H3K4me3 via its PHD finger and interacting with a DSB protein, Mer2. However, how the Spp1 PHD finger performs site-specific readout of H3K4me3 is still not fully understood. In the present study, we determined the crystal structure of the highly conserved Spp1 N-terminal domain (Sc_Spp1) in complex with the H3K4me3 peptide. The structure shows that Sc_Spp1 comprises a PHD finger responsible for methylated H3K4 recognition and a C3H-type zinc finger necessary to ensure the overall structural stability. Our isothermal titration calorimetry results show that binding of H3K4me3 to Sc_Spp1 is mildly inhibited by H3R2 methylation, weakened by H3T6 phosphorylation, and abrogated by H3T3 phosphorylation. This histone modification cross-talk, which is conserved in the and mammalian orthologs of Sc_Spp1 , can be rationalized structurally and might contribute to the roles of Spp1 in COMPASS activity regulation and meiotic recombination.

PubMed: 31253666
DOI: 10.1042/BCJ20190091

実験手法

X-RAY DIFFRACTION (2.85 Å)