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Author Correction: Sequence specificity analysis of the SETD2 protein lysine methyltransferase and discovery of a SETD2 super-substrate

Maren Kirstin Schuhmacher
Serap Beldar
Albert Jeltsch
Amendments and CorrectionsOpen Access19 Oct 2020
Communications Biology

Volume: 3, P: 1
Sequence specificity analysis of the SETD2 protein lysine methyltransferase and discovery of a SETD2 super-substrate

Schuhmacher, Beldar et al. design a super-substrate peptide based on the substrate sequence specificity of the SETD2 protein lysine methyltransferase. SETD2 methylates this super-substrate 290-fold more efficiently than the original H3K36 peptide. This study illustrates that substrate sequence design can improve the activity of protein lysine methyltransferases.

Maren Kirstin Schuhmacher
Serap Beldar
Albert Jeltsch
ResearchOpen Access16 Sept 2020
Communications Biology

Volume: 3, P: 1-13
Globally altered epigenetic landscape and delayed osteogenic differentiation in H3.3-G34W-mutant giant cell tumor of bone

The histone variant mutation H3.3-G34W occurs in the majority of giant cell tumor of bone (GCTB). By profiling patient-derived GCTB tumor cells, the authors show that this mutation associates with epigenetic alterations in heterochromatic and bivalent regions that contribute to an impaired osteogenic differentiation and the osteolytic phenotype of GCTB.

Pavlo Lutsik
Annika Baude
Christoph Plass
ResearchOpen Access27 Oct 2020
Nature Communications

Volume: 11, P: 1-16
The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes

Only very few enzymes are known to catalyze protein histidine methylation. Here, the authors show that METTL9 is responsible for most 1-methylhistidine modifications in mouse and human proteomes, and characterize METTL9′s substrate specificity and potential cellular functions.

Erna Davydova
Tadahiro Shimazu
Pål Ø. Falnes
ResearchOpen Access09 Feb 2021
Nature Communications

Volume: 12, P: 1-14
A loss-of-function variant in SUV39H2 identified in autism-spectrum disorder causes altered H3K9 trimethylation and dysregulation of protocadherin β-cluster genes in the developing brain

Shabeesh Balan
Yoshimi Iwayama
Takeo Yoshikawa
Research15 Jul 2021
Molecular Psychiatry

Volume: 26, P: 7550-7559

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Author Correction: Sequence specificity analysis of the SETD2 protein lysine methyltransferase and discovery of a SETD2 super-substrate

Sequence specificity analysis of the SETD2 protein lysine methyltransferase and discovery of a SETD2 super-substrate

Globally altered epigenetic landscape and delayed osteogenic differentiation in H3.3-G34W-mutant giant cell tumor of bone

The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes

A loss-of-function variant in SUV39H2 identified in autism-spectrum disorder causes altered H3K9 trimethylation and dysregulation of protocadherin β-cluster genes in the developing brain

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