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The Structural Basis for Specific Recognition of H3K14 Acetylation by Sth1 in the RSC Chromatin Remodeling Complex

Structure.. 2020-01; 
Chen G1, Li W1, Yan F1, Wang D1, Chen Y2.
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Peptide Synthesis … H2AK21Ac (ASQSRSAK Ac AGLTFPVY), Genscrip , China, N/A. H3K9Ac(ARTKQTARK(Ac) STGGKAPRKQLAS), Genscript , China, N/A. H3K14Ac (TARKSTGGK Ac APRKQLAY), Genscript , China, N/A. H3K18Ac(ARTKQTARKSTGGKAPRK Ac QLAS), Genscript , China, N/A … Get A Quote

摘要

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 (Sth1BD) possessed the strongest affinity to H3K14Ac among all RSC bromodomains. The Sth1BD specifically recognized the K(Ac)ΦΦR motif (Φ stands for any hydrophobic amino acid), including H3K14Ac and H4K20Ac. We determined the crystal structures of Sth1BD at 2.40 Å re... More

关键词

H3K14Ac; RSC complex; Sth1; bromodomain; chromatin remodeling; histone acetylation; structural biology, X-ray crystallography