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• W220595325 abstract "The lysine methyltransferase (KMT) SETMAR is implicated in the response to and repair of DNA damage, but its molecular function is not clear. SETMAR has been associated with dimethylation of histone H3 lysine 36 (H3K36) at sites of DNA damage. However, SETMAR does not methylate H3K36 in vitro. This and the observation that SETMAR is not active on nucleosomes suggest that H3K36 methylation is not a physiologically relevant activity. To identify potential non-histone substrates, we utilized a strategy on the basis of quantitative proteomic analysis of methylated lysine. Our approach identified lysine 130 of the mRNA splicing factor snRNP70 as a SETMAR substrate in vitro, and we show that the enzyme primarily generates monomethylation at this position. Furthermore, we show that SETMAR methylates snRNP70 Lys-130 in cells. Because snRNP70 is a key early regulator of 5′ splice site selection, our results suggest a model in which methylation of snRNP70 by SETMAR regulates constitutive and/or alternative splicing. In addition, the proteomic strategy described here is broadly applicable and is a promising route for large-scale mapping of KMT substrates.Background: SETMAR is a lysine methyltransferase (KMT) that contributes to DNA repair, but its biochemical function is not well understood.Results: A novel proteomic strategy identifies splicing factor snRNP70 as a SETMAR substrate.Conclusion: SETMAR is the first KMT identified to target splicing factors.Significance: Proteomics can be harnessed to discover methyltransferase substrates. Lysine methylation may be a new mode of regulation for mRNA splicing. The lysine methyltransferase (KMT) SETMAR is implicated in the response to and repair of DNA damage, but its molecular function is not clear. SETMAR has been associated with dimethylation of histone H3 lysine 36 (H3K36) at sites of DNA damage. However, SETMAR does not methylate H3K36 in vitro. This and the observation that SETMAR is not active on nucleosomes suggest that H3K36 methylation is not a physiologically relevant activity. To identify potential non-histone substrates, we utilized a strategy on the basis of quantitative proteomic analysis of methylated lysine. Our approach identified lysine 130 of the mRNA splicing factor snRNP70 as a SETMAR substrate in vitro, and we show that the enzyme primarily generates monomethylation at this position. Furthermore, we show that SETMAR methylates snRNP70 Lys-130 in cells. Because snRNP70 is a key early regulator of 5′ splice site selection, our results suggest a model in which methylation of snRNP70 by SETMAR regulates constitutive and/or alternative splicing. In addition, the proteomic strategy described here is broadly applicable and is a promising route for large-scale mapping of KMT substrates. Background: SETMAR is a lysine methyltransferase (KMT) that contributes to DNA repair, but its biochemical function is not well understood. Results: A novel proteomic strategy identifies splicing factor snRNP70 as a SETMAR substrate. Conclusion: SETMAR is the first KMT identified to target splicing factors. Significance: Proteomics can be harnessed to discover methyltransferase substrates. Lysine methylation may be a new mode of regulation for mRNA splicing." @default.
• W220595325 created "2016-06-24" @default.
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• W220595325 date "2015-05-01" @default.
• W220595325 modified "2023-10-18" @default.
• W220595325 title "A Proteomic Strategy Identifies Lysine Methylation of Splicing Factor snRNP70 by the SETMAR Enzyme" @default.
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• W220595325 doi "https://doi.org/10.1074/jbc.m115.641530" @default.
• W220595325 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4424340" @default.
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