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Article Abstract
Histone monoaminylation (., serotonylation and dopaminylation) is an emerging category of epigenetic mark occurring on the fifth glutamine (Q5) residue of H3 N-terminal tail, which plays significant roles in gene transcription. Current analysis of histone monoaminylation is mainly based on site-specific antibodies and mass spectrometry, which either lacks high resolution or is time-consuming. In this study, we report the development of chemical probes for bioorthogonal labeling and enrichment of histone serotonylation and dopaminylation. These probes were successfully applied for the monoaminylation analysis of biochemical assays, cells, and tissue samples. The enrichment of monoaminylated histones by the probes further confirmed the crosstalk between H3Q5 monoaminylation and H3K4 methylation. Finally, combining the and analyses based on the developed probes, we have shown that both histone serotonylation and dopaminylation are highly enriched in tumor tissues that overexpress transglutaminase 2 (TGM2) and regulate the three-dimensional architecture of cellular chromatin.
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Article Synopsis
- Scientists discovered a new way to study how proteins in the brain can be changed after they're made, specifically focusing on a type called "dopaminylation."
- They found over 1,500 proteins that have this change, many of which are important for sending signals in brain cells and helping with memory.
- One protein, called γCaMKII, plays a big role in helping neurons talk to each other and might be important for learning and adapting to new situations.