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Limited choice of natural amino acids as mimetics restricts design of protein lysine methylation studies

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  • Sara Weirich

    (University of Stuttgart)

  • Albert Jeltsch

    (University of Stuttgart)

Abstract

Protein lysine methylation plays important biological roles but its experimental characterization is limited by the lack of suitable mimetics of methylated and unmethylated lysine among the natural amino acids. Here, we summarize the consequent challenges and discuss alternative approaches for biochemical and cellular lysine methylation studies.

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  • Sara Weirich & Albert Jeltsch, 2023. "Limited choice of natural amino acids as mimetics restricts design of protein lysine methylation studies," Nature Communications, Nature, vol. 14(1), pages 1-3, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-39777-8
    DOI: 10.1038/s41467-023-39777-8
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    References listed on IDEAS

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    1. Bo Yu & Jun Su & Qiqi Shi & Qing Liu & Jun Ma & Guoqing Ru & Lei Zhang & Jian Zhang & Xichun Hu & Jianming Tang, 2022. "KMT5A-methylated SNIP1 promotes triple-negative breast cancer metastasis by activating YAP signaling," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Neil Justin & Ying Zhang & Cataldo Tarricone & Stephen R. Martin & Shuyang Chen & Elizabeth Underwood & Valeria De Marco & Lesley F. Haire & Philip A. Walker & Danny Reinberg & Jon R. Wilson & Steven , 2016. "Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2," Nature Communications, Nature, vol. 7(1), pages 1-11, September.
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