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- W3016585357 abstract "Lysine methylation is a protein post-translational modification (PTMs) that can affect protein stability, activity, subcellular localization, and molecular interactions. Revealing protein substrates for lysine methyltransferases (KMTs) will help connect enzymatic activity to cellular functions and pathologies associated with these enzymes. Toward this goal, we developed a high-throughput screening assay to define the sequence determinants of KMT substrate selectivity. This assay queries a highly degenerate lysine-oriented peptide library (K-OPL) to identify amino acid preferences at three resides N- and C-terminal to a fixed central lysine. Here, we demonstrate the utility of this approach to facilitate identification of several novel substrates of KMT activity, including for SMYD1 (SET and MYND domain-containing protein 1), a KMT expressed in cardiac and skeletal muscle that is essential for heart development and organ homeostasis. We further demonstrate the utility of this tool, in conjunction with in silico and biophysical approaches, for revealing the impact of a cardiac disease-associated mutation of SMYD1 on its KMT function. Collectively, our studies reveal new hypotheses toward a better understanding of SMYD1 function in cardiac and skeletal muscle development and implicate its aberrant KMT activity in heart disease. Support or Funding Information NIH R356M14736" @default.
- W3016585357 created "2020-04-24" @default.
- W3016585357 creator A5033901454 @default.
- W3016585357 date "2020-04-01" @default.
- W3016585357 modified "2023-09-23" @default.
- W3016585357 title "Revealing the sequence determinants of SMYD1 lysine methyltransferase substrate selectivity with lysine‐oriented peptide libraries" @default.
- W3016585357 doi "https://doi.org/10.1096/fasebj.2020.34.s1.08943" @default.
- W3016585357 hasPublicationYear "2020" @default.
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