Investigation of H2AX methylation by the SUV39H2 protein lysine methyltransferase

The H3K9 protein lysine methyltransferase SUV39H2 was reported to methylate K134 of H2AX and stimulate H2AX phosphorylation during DNA damage response [Sone K et al. (2014) Nat Commun 5, 5691]. However, the sequence context of H2AX‐K134 differs from the specificity of SUV39H2. We performed in vitro...

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Bibliographic Details
Published inFEBS letters Vol. 590; no. 12; pp. 1713 - 1719
Main Authors Schuhmacher, Maren Kirstin, Kudithipudi, Srikanth, Jeltsch, Albert
Format Journal Article
LanguageEnglish
Published England 01.06.2016
Subjects
DNA repair
enzyme specificity
H2AX
Histone-Lysine N-Methyltransferase - chemistry
Histone-Lysine N-Methyltransferase - genetics
Histone-Lysine N-Methyltransferase - metabolism
Histones - chemistry
Histones - genetics
Histones - metabolism
Humans
Methylation
peptide recognition
protein lysine methylation
Substrate Specificity
SUV39H2
H2AX
SUV39H2
peptide recognition
enzyme specificity
protein lysine methylation
DNA repair
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Summary:The H3K9 protein lysine methyltransferase SUV39H2 was reported to methylate K134 of H2AX and stimulate H2AX phosphorylation during DNA damage response [Sone K et al. (2014) Nat Commun 5, 5691]. However, the sequence context of H2AX‐K134 differs from the specificity of SUV39H2. We performed in vitro methylation reactions with SUV39H2 (and its homolog SUV39H1) using H2AX protein and peptides, but no methylation at K134 or any other lysine in H2AX was detected. Positive controls demonstrated the functionality of the assays. While our data cannot finally exclude H2AX methylation of SUV39H2 in cells, additional experimental evidence is required to validate this claim.
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ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.12216