ArticleNature chemical biology2025
Mechanism of nucleosomal H2A K13/15 monoubiquitination and adjacent dual monoubiquitination by RNF168.
Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Precision Chemistry for Protein Lysine Modification.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Steric Gating Contributes to the Preferential Ubiquitin Charging of BIRC6 by UBA6 versus UBA1.Nature communications · 2026Article
- Unique gluing effect of ASXL1 K351 monoubiquitination stimulates the PR-DUB activity.Nature chemical biology · 2026Article
- Allosteric activation of RNF20/RNF40-RAD6A-mediated H2BK120 monoubiquitylation by H2BS112 GlcNAcylation.Nature chemical biology · 2026Article
- Structural basis for E4 enzyme Ufd2-catalyzed K48/K29 branched ubiquitin chains.Nature chemical biology · 2026Article
- E2 variants for probing E3 ubiquitin ligase activities.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- EnP1 exploits H2Aub-dependent epigenetic reprogramming to promote microsporidia proliferation in host cells.PLoS pathogens · 2026Article
- Design and Semisynthesis of Ubiquitin Extension Probes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Post-translational modification of H2B C-terminal helix regulates nucleosome interactions and chromatin signaling.Nucleic acids research · 2025Article
- AlphaFold-guided structural analyses of nucleosome binding proteins.Nucleic acids research · 2025Article
- Structural visualization of HECT-type E3 ligase Ufd4 accepting and transferring ubiquitin to form K29/K48-branched polyubiquitination.Nature communications · 2025Article
- Review
- Ubiquitination-mediated protein homeostasis in cardiovascular diseases: molecular mechanisms and therapeutic opportunities.American journal of cardiovascular disease · 2025Review
- LPS gets a fresh trim.Nature chemical biology · 2024Article
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Authors and funding
17 authors.
Funding
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Abstract
The DNA damage repair regulatory protein RNF168, a monomeric RING-type E3 ligase, has a crucial role in regulating cell fate and DNA repair by specific and efficient ubiquitination of the adjacent K13 and K15 (K13/15) sites at the H2A N-terminal tail. However, understanding how RNF168 coordinates with its cognate E2 enzyme UbcH5c to site-specifically ubiquitinate H2A K13/15 has long been hampered by the lack of high-resolution structures of RNF168 and UbcH5c~Ub (ubiquitin) in complex with nucleosomes. Here we developed chemical strategies and determined the cryo-electron microscopy structures of the RNF168-UbcH5c~Ub-nucleosome complex captured in transient H2A K13/15 monoubiquitination and adjacent dual monoubiquitination reactions, providing a 'helix-anchoring' mode for monomeric E3 ligase RNF168 on nucleosome in contrast to the 'compass-binding' mode of dimeric E3 ligases. Our work not only provides structural snapshots of H2A K13/15 site-specific monoubiquitination and adjacent dual monoubiquitination but also offers a near-atomic-resolution structural framework for understanding pathogenic amino acid substitutions and physiological modifications of RNF168.
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