ArticleCommunications biology2020
Sequence specificity analysis of the SETD2 protein lysine methyltransferase and discovery of a SETD2 super-substrate.
Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- The SETD2 L1609P mutation found in leukemia disrupts methyltransferase activity and reduces histone H3K36 trimethylation.The Journal of biological chemistry · 2026Article
- Stapled histone H3 tails are super-substrates for lysine methyltransferase SETD7.Chemical science · 2026Article
- Mechanisms of Substrate Recognition by the Multispecific Protein Lysine Methyltransferase SETD6.Life (Basel, Switzerland) · 2025Article
- Emergent properties of the lysine methylome reveal regulatory roles via protein interactions and histone mimicry.Epigenomics · 2025Article
- Discovery of NSD2 non-histone substrates and design of a super-substrate.Communications biology · 2024Article
- Limited choice of natural amino acids as mimetics restricts design of protein lysine methylation studies.Nature communications · 2023Article
- Histone methyltransferase SETD2: An epigenetic driver in clear cell renal cell carcinoma.Frontiers in oncology · 2023Review
- Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide.Communications chemistry · 2022Article
- Structural and functional specificity of H3K36 methylation.Epigenetics & chromatin · 2022Review
- Lysine methyltransferase inhibitors: where we are now.RSC chemical biology · 2022Review
- Histone methyltransferases SDG33 and SDG34 regulate organ-specific nitrogen responses in tomato.Frontiers in plant science · 2022Article
- Specificity Analysis of Protein Methyltransferases and Discovery of Novel Substrates Using SPOT Peptide Arrays.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Surprising phenotypic diversity of cancer-associated mutations of Gly 34 in the histone H3 tail.eLife · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 2 institutions in 3 countries.
Funding
Abstract
SETD2 catalyzes methylation at lysine 36 of histone H3 and it has many disease connections. We investigated the substrate sequence specificity of SETD2 and identified nine additional peptide and one protein (FBN1) substrates. Our data showed that SETD2 strongly prefers amino acids different from those in the H3K36 sequence at several positions of its specificity profile. Based on this, we designed an optimized super-substrate containing four amino acid exchanges and show by quantitative methylation assays with SETD2 that the super-substrate peptide is methylated about 290-fold more efficiently than the H3K36 peptide. Protein methylation studies confirmed very strong SETD2 methylation of the super-substrate in vitro and in cells. We solved the structure of SETD2 with bound super-substrate peptide containing a target lysine to methionine mutation, which revealed better interactions involving three of the substituted residues. Our data illustrate that substrate sequence design can strongly increase the activity of protein lysine methyltransferases.
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