Substrates: SUVR4 protein shows very low histone methyltransferase activity against the unmethylated histone H3 1-20 peptide. SUVR4 is also unable to methylate H3 1-20 peptides monomethylated at K4 or dimethylated at K9. SUVR4 is able to methylate histone H3 peptides of variable size when monomethylated at K9, but not when monomethylated at K4 or K27 or dimethylated on K9 Products: -
Substrates: in the absence of ubiquitin, SUVR4 converts 40.9% of the H3K9me1 peptide to H3K9me2, while 0% is converted to H3K9me3. In the presence of ubiquitin, 90.2% of the H3K9me1 peptide is converted to H3K9me2 while 3.5% is converted to H3K9me3. When H3K9me2 peptides are used as substrate, there is no conversion to H3K9me3 above background level in the absence of ubiquitin. When ubiquitin is present together with SUVR4, a 16.4% conversion from H3K9me2 to H3K9me3 is found Products: -
addition of free ubiquitin stimulates enzymatic activity of the SUVR4 protein on histone H3 but does not affect its specificity. In presence of ubiquitin, methylation of H3K9me1 modified peptides increases 2.5-3fold. Trimethylation of the H3K9me2 peptide is observed in the presence of ubiquitin
at least two different transcripts are expressed. SUVR4a contains 9 exons with an ORF of 1395 bp (465 amino acids). Alternative splice variant, SUVR4b, retains the 81 bp second intron, resulting in an ORF of 1476 bp
the N-terminal WIYLD domain of the SUVR4 HKMTase binds ubiquitin and the SUVR4 product specificity shifts from di- to trimethylation in the presence of free ubiquitin, enabling conversion of H3K9me1 to H3K9me3 in vitro. SUVR4 in vivo specifically converts H3K9me1 to H3K9me3 at transposons and pseudogenes and has a locus-specific repressive effect on the expression of such elements. This repression involves both DNA methylation-dependent and -independent mechanisms
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
SUVR4 WIYLD-domain is a domain with a four-helix bundle structure binding ubiquitin. Residues of helix alpha1 (Q38, L39, and D40) and helix alpha4 (N68, T70, A71, V73, D74, I76, S78, and E82) of WIYLD and residues between the first and second beta-strands (T9 and G10) and on beta-strands 3 (R42, G47, K48, and Q49) and 4 (H68, R72, and L73) undergo significant chemical shift changes when the two proteins interact
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