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IUBMB CommentsThis entry describes enzymes that methylate the L-lysine-27 residue of histone H3 only once, generating a monomethylated form. This modification influences the binding of chromatin-associated proteins. The methylation of lysine-27 leads to transcriptional repression of the affected target genes. cf. EC 2.1.1.371, [histone H3]-lysine27 N-dimethyltransferase, and EC 2.1.1.356, [histone H3]-lysine27 N-trimethyltransferase.
Synonyms
atxr5, atxr6, arabidopsis trithorax-related protein 5, arabidopsis trithorax-related protein5, set15, set34,
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S-adenosyl-L-methionine + [histone H3.1 peptide KAARKSAPATVGGK]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3.1 peptide KAARK*SAPATVGGK]-N6-methyl-L-lysine27
peptide corresponds to residues K23-K36
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S-adenosyl-L-methionine + [histone H3.1]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3.1]-N6-methyl-L-lysine27
S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
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S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
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S-adenosyl-L-methionine + [histone H3.1]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3.1]-N6-methyl-L-lysine27
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S-adenosyl-L-methionine + [histone H3.1]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3.1]-N6-methyl-L-lysine27
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S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
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S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
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isoforms Atxr5 and Atxr6 specifically monomethylate histone H3K27
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isoforms Atxr5 and Atxr6 specifically monomethylate histone H3K27
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additional information
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isoforms Atxr5 and Atxr6 specifically monomethylate histone H3K27
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additional information
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K27Q mutation in variant H3.3 further aggravates the replication stress phenotype of K27Q mutation in canonical H3. H3.3 is a physiologically relevant substrate of TXR1
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physiological function
isoforms ATXR5 and ATXR6 exhibit histone H3K27 monomethyltransferase activity and double mutants have reduced H3K27me1 levels in vivo and show partial heterochromatin decondensation. Mutations in Atxr5 and Atxr6 also lead to transcriptional activation of repressed heterochromatic elements. H3K9me2 and DNA methylation are unaffected in the double mutant
physiological function
ATXR5 selectively methylates the replication-dependent histone H3 variant H3.1. ATXR5 contains a bipartite catalytic domain that specifically reads alanine-31 of H3.1. Variation at position 31 between H3.1 and replication-independent H3.3 is conserved in plants and animals, and threonine-31 in H3.3 is responsible for inhibiting the activity of ATXR5 and its paralog, ATXR6
physiological function
ATXR6 associates with proliferating cell nuclear antigen PCNA, and PCNA inhibits ATXR6 enzymatic activity. A trio of hydrophobic residues contributes to the binding of the enzyme to the sliding clamp of PCNA. ATXR6 PIP motif participates in the binding of PCNA and two molecules of ATXR6 bind to a trimer of PCNA likely enabling the recruitment of a third protein to the sliding clamp
physiological function
isoform ATXR5 discriminates between histone H3 variants and preferentially methylates K27 on histone H3.1. ATXR5 preferentially methylates the R/F-K*-S/C-G/A-P/C motif with striking preference for hydrophobic and aromatic residues in positions flanking this core of five amino acids. Posttranscriptional modifications of residues neighboring K27 that are typically associated with actively transcribed chromatin are detrimental to ATXR5 activity. The ATXR5 PHD domain employs a narrow binding pocket to selectively recognize unmethylated K4 of histone H3. Deletion or mutation of the PHD domain reduces the catalytic efficiency of ATXR5 up to 58fold
physiological function
isoforms ATXR5 and ATXR6 interact with RNA metabolism component serrate. Serrate binds to ATXR5/6-regulated transposable elements loci and promotes H3K27me1 accumulation in these regions. Serrate directly enhances ATXR5 enzymatic activity in vitro. Serrate mutation suppresses the transposable elements reactivation and DNA rereplication phenotypes in the Atxr5/Atxr6 mutant through RDR6
physiological function
mutation of isoforms ATXR5 and ATXR6 lead to rereplication of specific genomic locations, the vast majority of which correspond to transposons and other repetitive and silent elements of the Arabidopsis genome. These sites also correspond to high levels of H3K27 monomethylation. Mutation of ATXR5 and ATXR6 also causes upregulation of transposon expression and has pleiotropic effects on plant development
physiological function
mutation of isoforms ATXR5 and ATXR6 lead to rereplication of specific genomic locations, the vast majority of which correspond to transposons and other repetitive and silent elements of the Arabidopsis genome. These sites also correspond to high levels of H3K27 monomethylation. Mutation of ATXR5 and ATXR6 also causes upregulation of transposon expression and has pleiotropic effects on plant development. The PIP motif, PHD and SET domains are all required for ATXR6 activity
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Zhao, X.; Wang, Y.; Wang, Y.; Liu, Y.; Gao, S.
Histone methyltransferase TXR1 is required for both H3 and H3.3 lysine 27 methylation in the well-known ciliated protist Tetrahymena thermophila
Sci. China Life Sci.
60
264-270
2017
Tetrahymena thermophila
brenda
Jacob, Y.; Feng, S.; LeBlanc, C.A.; Bernatavichute, Y.V.; Stroud, H.; Cokus, S.; Johnson, L.M.; Pellegrini, M.; Jacobsen, S.E.;Michaels, S.D.
ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing
Nat. Struct. Mol. Biol.
16
763-768
2009
Arabidopsis thaliana (Q8VZJ1), Arabidopsis thaliana (Q9FNE9), Arabidopsis thaliana
brenda
Ma, Z.; Castillo-Gonzalez, C.; Wang, Z.; Sun, D.; Hu, X.; Shen, X.; Potok, M.E.; Zhang, X.
Arabidopsis serrate coordinates histone methyltransferases ATXR5/6 and RNA processing factor RDR6 to regulate transposon expression
Dev. Cell
45
769-784.e6
2018
Arabidopsis thaliana (Q8VZJ1), Arabidopsis thaliana (Q9FNE9)
brenda
Davarinejad, H.; Joshi, M.; Ait-Hamou, N.; Munro, K.; Couture, J.F.
ATXR5/6 forms alternative protein complexes with PCNA and the nucleosome core particle
J. Mol. Biol.
431
1370-1379
2019
Arabidopsis thaliana (Q9FNE9)
brenda
Jacob, Y.; Stroud, H.; Leblanc, C.; Feng, S.; Zhuo, L.; Caro, E.; Hassel, C.; Gutierrez, C.; Michaels, S.D.; Jacobsen, S.E.
Regulation of heterochromatic DNA replication by histone H3 lysine 27 methyltransferases
Nature
466
987-991
2010
Arabidopsis thaliana (Q8VZJ1), Arabidopsis thaliana (Q9FNE9)
brenda
Bergamin, E.; Sarvan, S.; Malette, J.; Eram, M.S.; Yeung, S.; Mongeon, V.; Joshi, M.; Brunzelle, J.S.; Michaels, S.D.; Blais, A.; Vedadi, M.; Couture, J.F.
Molecular basis for the methylation specificity of ATXR5 for histone H3
Nucleic Acids Res.
45
6375-6387
2017
Ricinus communis (B9RU15)
brenda
Jacob, Y.; Bergamin, E.; Donoghue, M.T.; Mongeon, V.; LeBlanc, C.; Voigt, P.; Underwood, C.J.; Brunzelle, J.S.; Michaels, S.D.; Reinberg, D.; Couture, J.F.; Martienssen, R.A.
Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication
Science
343
1249-1253
2014
Arabidopsis thaliana (Q8VZJ1)
brenda