4NJ5

Crystal structure of SUVH9

Summary for 4NJ5

• Entry DOI: 10.2210/pdb4nj5/pdb
• Descriptor: Probable histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH9, ZINC ION (3 entities in total)
• Functional Keywords: set domain, zinc binding motif, zinc binding, metal binding protein
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Cellular location: Nucleus (By similarity): Q9T0G7
• Total number of polymer chains: 1
• Total formula weight: 58199.66

Authors

Du, J.,Patel, D.J. (deposition date: 2013-11-08, release date: 2014-01-22, Last modification date: 2024-02-28)

Primary citation

Johnson, L.M.,Du, J.,Hale, C.J.,Bischof, S.,Feng, S.,Chodavarapu, R.K.,Zhong, X.,Marson, G.,Pellegrini, M.,Segal, D.J.,Patel, D.J.,Jacobsen, S.E.
SRA- and SET-domain-containing proteins link RNA polymerase V occupancy to DNA methylation.
Nature, 507:124-128, 2014

PubMed Abstract: RNA-directed DNA methylation in Arabidopsis thaliana depends on the upstream synthesis of 24-nucleotide small interfering RNAs (siRNAs) by RNA POLYMERASE IV (Pol IV) and downstream synthesis of non-coding transcripts by Pol V. Pol V transcripts are thought to interact with siRNAs which then recruit DOMAINS REARRANGED METHYLTRANSFERASE 2 (DRM2) to methylate DNA. The SU(VAR)3-9 homologues SUVH2 and SUVH9 act in this downstream step but the mechanism of their action is unknown. Here we show that genome-wide Pol V association with chromatin redundantly requires SUVH2 and SUVH9. Although SUVH2 and SUVH9 resemble histone methyltransferases, a crystal structure reveals that SUVH9 lacks a peptide-substrate binding cleft and lacks a properly formed S-adenosyl methionine (SAM)-binding pocket necessary for normal catalysis, consistent with a lack of methyltransferase activity for these proteins. SUVH2 and SUVH9 both contain SRA (SET- and RING-ASSOCIATED) domains capable of binding methylated DNA, suggesting that they function to recruit Pol V through DNA methylation. Consistent with this model, mutation of DNA METHYLTRANSFERASE 1 (MET1) causes loss of DNA methylation, a nearly complete loss of Pol V at its normal locations, and redistribution of Pol V to sites that become hypermethylated. Furthermore, tethering SUVH9 [corrected] with a zinc finger to an unmethylated site is sufficient to recruit Pol V and establish DNA methylation and gene silencing. These results indicate that Pol V is recruited to DNA methylation through the methyl-DNA binding SUVH2 and SUVH9 proteins, and our mechanistic findings suggest a means for selectively targeting regions of plant genomes for epigenetic silencing.

PubMed: 24463519
DOI: 10.1038/nature12931

Experimental method

X-RAY DIFFRACTION (2.4 Å)