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Mechanism of DNA methylation-directed histone methylation by KRYPTONITE.

Du J, Johnson LM, Groth M, Feng S, Hale CJ, Li S, Vashisht AA, Wohlschlegel JA, Patel DJ, Jacobsen SE, Jacobsen SE
Mol Cell 55 495-504 (2014)
Related entries: 4qeo, 4qep

Cited: 98 times
EuropePMC logo PMID: 25018018

Abstract

In Arabidopsis, CHG DNA methylation is controlled by the H3K9 methylation mark through a self-reinforcing loop between DNA methyltransferase CHROMOMETHYLASE3 (CMT3) and H3K9 histone methyltransferase KRYPTONITE/SUVH4 (KYP). We report on the structure of KYP in complex with methylated DNA, substrate H3 peptide, and cofactor SAH, thereby defining the spatial positioning of the SRA domain relative to the SET domain. The methylated DNA is bound by the SRA domain with the 5mC flipped out of the DNA, while the H3(1-15) peptide substrate binds between the SET and post-SET domains, with the ε-ammonium of K9 positioned adjacent to bound SAH. These structural insights, complemented by functional data on key mutants of residues lining the 5mC and H3K9-binding pockets within KYP, establish how methylated DNA recruits KYP to the histone substrate. Together, the structures of KYP and previously reported CMT3 complexes provide insights into molecular mechanisms linking DNA and histone methylation.

Reviews - 4qen mentioned but not cited (1)

  1. DNA methylation pathways and their crosstalk with histone methylation. Du J, Johnson LM, Jacobsen SE, Patel DJ. Nat Rev Mol Cell Biol 16 519-532 (2015)

Articles - 4qen mentioned but not cited (3)

  1. Mechanism of DNA methylation-directed histone methylation by KRYPTONITE. Du J, Johnson LM, Groth M, Feng S, Hale CJ, Li S, Vashisht AA, Wohlschlegel JA, Patel DJ, Jacobsen SE. Mol Cell 55 495-504 (2014)
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