6A5K

Crystal structure of Arabidopsis thaliana SUVH6 in complex with SAM, form 1

6A5K の概要

• エントリーDOI: 10.2210/pdb6a5k/pdb
• 分子名称: Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH6, ZINC ION, S-ADENOSYLMETHIONINE, ... (4 entities in total)
• 機能のキーワード: sra, set, histone methyltransferase, dna methylation, gene regulation
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60097.30

構造登録者

Li, X.,Du, J. (登録日: 2018-06-24, 公開日: 2018-08-29, 最終更新日: 2018-09-26)

主引用文献

Li, X.,Harris, C.J.,Zhong, Z.,Chen, W.,Liu, R.,Jia, B.,Wang, Z.,Li, S.,Jacobsen, S.E.,Du, J.
Mechanistic insights into plant SUVH family H3K9 methyltransferases and their binding to context-biased non-CG DNA methylation.
Proc. Natl. Acad. Sci. U.S.A., 115:E8793-E8802, 2018

PubMed Abstract: DNA methylation functions in gene silencing and the maintenance of genome integrity. In plants, non-CG DNA methylation is linked through a self-reinforcing loop with histone 3 lysine 9 dimethylation (H3K9me2). The plant-specific SUPPRESSOR OF VARIEGATION 3-9 HOMOLOG (SUVH) family H3K9 methyltransferases (MTases) bind to DNA methylation marks and catalyze H3K9 methylation. Here, we analyzed the structure and function of SUVH6 to understand how this class of enzyme maintains methylation patterns in the genome. We reveal that SUVH6 has a distinct 5-methyl-dC (5mC) base-flipping mechanism involving a thumb loop element. Autoinhibition of H3 substrate entry is regulated by a SET domain loop, and a conformational transition in the post-SET domain upon cofactor binding may control catalysis. In vitro DNA binding and in vivo ChIP-seq data reveal that the different SUVH family H3K9 MTases have distinct DNA binding preferences, targeting H3K9 methylation to sites with different methylated DNA sequences, explaining the context biased non-CG DNA methylation in plants.

PubMed: 30150382
DOI: 10.1073/pnas.1809841115

実験手法

X-RAY DIFFRACTION (1.9 Å)