Using dimethylsulfonium to identify readers of methylation

Decoding a post-translational modification requires the identification of its ‘reader’ proteins. Now a method can covalently trap the readers of lysine methylation using dimethylsulfonium as a methyllysine-mimicking ‘warhead’ to crosslink the tryptophan residues inside the binding pocket.

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Bibliographic Details
Published inNature chemistry Vol. 16; no. 8; pp. 1221 - 1222
Main Authors Li, Xiang, Li, Xiang David
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 01.08.2024
Nature Publishing Group
Subjects
639/638/403/933
639/638/92/458/1648
Analytical Chemistry
Binding sites
Biochemistry
Chemical bonds
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Epigenetics
Humans
Inorganic Chemistry
Labeling
Lysine
Methylation
News & Views
news-and-views
Organic Chemistry
Peptides
Physical Chemistry
Post-translation
Proteins
Proteomics
Sulfonium Compounds - chemistry
Tryptophan
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Summary:Decoding a post-translational modification requires the identification of its ‘reader’ proteins. Now a method can covalently trap the readers of lysine methylation using dimethylsulfonium as a methyllysine-mimicking ‘warhead’ to crosslink the tryptophan residues inside the binding pocket.
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ISSN:1755-4330
1755-4349
1755-4349
DOI:10.1038/s41557-024-01582-1