Chemical proteomic profiling of lysine crotonylation using minimalist bioorthogonal probes in mammalian cells.

ABSTRACT: Protein lysine crotonylation has been found to be closely related to the occurrence and development of various diseases. Currently, site identification of crotonylation is mainly dependent on antibody enrichment; however, due to the cost, heterogeneity, and specificity of antibodies, it is desired to develop an alternative chemical tool to detect crotonylation. Herein, we report an alkynyl-functionalized bioorthogonal chemical probe, Cr-alkyne, for the detection and identification of protein lysine crotonylation in mammalian cells. Our in-gel fluorescence and chemical proteomic analyses demonstrated that Cr-alkyne can be metabolically incorporated into lysine of histones and directly label known crotonylated proteins. We further applied Cr-alkyne to the proteome-wide profiling of crotonyla

SUBMITTER: Zhou YF 

PROVIDER: S-EPMC11730115 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature