6KMJ

Crystal structure of Sth1 bromodomain in complex with H3K14Ac

Summary for 6KMJ

• Entry DOI: 10.2210/pdb6kmj/pdb
• Related: 6KMB
• Descriptor: Nuclear protein STH1/NPS1, Histone H3, GLYCEROL, ... (4 entities in total)
• Functional Keywords: chromatin remodeling, histone acetylation, rsc complex, sth1, bromodomain, gene regulation
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 15306.22

Authors

Chen, G.,Li, W.,Yan, F.,Wang, D.,Chen, Y. (deposition date: 2019-07-31, release date: 2019-11-27, Last modification date: 2024-11-06)

Primary citation

Chen, G.,Li, W.,Yan, F.,Wang, D.,Chen, Y.
The Structural Basis for Specific Recognition of H3K14 Acetylation by Sth1 in the RSC Chromatin Remodeling Complex.
Structure, 28:111-, 2020

PubMed Abstract: The Saccharomyces cerevisiae RSC (Remodel the Structure of Chromatin) complex is a chromatin-remodeling complex and plays essential roles in transcription regulation and DNA repair. The acetylation of H3 Lysine14 (H3K14Ac) enhances the RSC retention on nucleosomes and increases the remodeling activity of RSC. However, which RSC component recognizes H3K14Ac remains unclear. Here, we discovered that the bromodomain of the catalytic subunit Sth1 (Sth1) possessed the strongest affinity to H3K14Ac among all RSC bromodomains. The Sth1 specifically recognized the K(Ac)ΦΦR motif (Φ stands for any hydrophobic amino acid), including H3K14Ac and H4K20Ac. We determined the crystal structures of Sth1 at 2.40 Å resolution and Sth1-H3K14Ac complex at 1.40 Å resolution. The extensive interfaces between Sth1 and H3 facilitate the specific and robust binding of Sth1 to H3K14Ac. Our studies provide insights into how the RSC complex recognizes H3K14Ac to orchestrate the crosstalk between histone acetylation and chromatin remodeling.

PubMed: 31711754
DOI: 10.1016/j.str.2019.10.015

Experimental method

X-RAY DIFFRACTION (1.4 Å)