Uncoupling histone modification crosstalk by engineering lysine demethylase LSD1

Biochemical crosstalk between two or more histone modifications is often observed in epigenetic enzyme regulation, but its functional significance in cells has been difficult to discern. Previous enzymatic studies revealed that Lys14 acetylation of histone H3 can inhibit Lys4 demethylation by lysine...

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Veröffentlicht in:	Nature chemical biology 2024-07, Vol.21 (2), p.227-237
Hauptverfasser:	Lee, Kwangwoon, Barone, Marco, Waterbury, Amanda L., Jiang, Hanjie, Nam, Eunju, DuBois-Coyne, Sarah E., Whedon, Samuel D., Wang, Zhipeng A., Caroli, Jonatan, Neal, Katherine, Ibeabuchi, Brian, Dhoondia, Zuzer, Kuroda, Mitzi I., Liau, Brian B., Beck, Samuel, Mattevi, Andrea, Cole, Philip A.
Format:	Artikel
Sprache:	eng
Schlagworte:	631/45/612/100/2285 631/92/607 Acetylation Biochemical Engineering Biochemistry Bioorganic Chemistry Cell activation Cell adhesion Cell Biology Chemistry Chemistry and Materials Science Chemistry/Food Science Chromatin CRISPR Demethylation Enzymes Epigenesis, Genetic Epigenetics Gene silencing Genes Histone Demethylases - genetics Histone Demethylases - metabolism Histone H3 Histones Histones - genetics Histones - metabolism Humans K562 Cells Lysine Lysine - metabolism Mutants Protein Engineering Regulatory sequences Transcription activation
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