biostudies-literatureAlAfaleq NONCI NIH HHSNIGMS NIH HHS1238154https://www.ebi.ac.uk/biostudies/studies/S-EPMC11952697biostudies-literatureUnknown1The attachment of mono-ubiquitin to histones as a post-translational modification plays important roles in regulating chromatin structure and function. Like other epigenetic modifications, the site of ubiquitin attachment is critically important in determining its functional outcome. Depending on the type of histone and the specific lysine residue that is modified, ubiquitination acts in diverse pathways including DNA damage repair, transcription elongation, and transcription repression. Specific reader, writer and eraser activities have evolved to distinguish nucleosomes by ubiquitination of different sites. To facilitate biochemical studies of ubiquitinated nucleosomes, we have developed an efficient strategy to chemically ligate intact ubiquitin and histone proteins at specific sites toFrontiers in epigenetics and epigenomicsGeneration of site-specific ubiquitinated histones through chemical ligation to probe the specificities of histone deubiquitinases.PMC11952697R01 GM115997R01 CA272771R01 GM098401Cohen REYao TAlAfaleq NOAtanassov BSChoi YSfalseGeneration of site-specific ubiquitinated histones through chemical ligation to probe the specificities of histone deubiquitinases.The attachment of mono-ubiquitin to histones as a post-translational modification plays important roles in regulating chromatin structure and function. Like other epigenetic modifications, the site of ubiquitin attachment is critically important in determining its functional outcome. Depending on the type of histone and the specific lysine residue that is modified, ubiquitination acts in diverse pathways including DNA damage repair, transcription elongation, and transcription repression. Specific reader, writer and eraser activities have evolved to distinguish nucleosomes by ubiquitination of different sites. To facilitate biochemical studies of ubiquitinated nucleosomes, we have developed an efficient strategy to chemically ligate intact ubiquitin and histone proteins at specific sites to2023-01-01T00:00:00Z20232026-06-02T20:37:41.404Z2026-04-20T03:10:13.349ZS-EPMC119526974016084710.3389/freae.2023.1238154