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From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/H2A1B_HUMAN H2A1B_HUMAN] | [https://www.uniprot.org/uniprot/H2A1B_HUMAN H2A1B_HUMAN] | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Histone H2B monoubiquitylation plays essential roles in chromatin-based transcriptional processes. A RING-type E3 ligase (yeast Bre1 or human RNF20/RNF40) and an E2 ubiquitin-conjugating enzyme (yeast Rad6 or human hRAD6A), together, precisely deposit ubiquitin on H2B K123 in yeast or K120 in humans. Here, we developed a chemical trapping strategy and successfully captured the transient structures of Bre1- or RNF20/RNF40-mediated ubiquitin transfer from Rad6 or hRAD6A to nucleosomal H2B. Our structures show that Bre1 and RNF40 directly bind nucleosomal DNA, exhibiting a conserved E3/E2/nucleosome interaction pattern from yeast to humans for H2B monoubiquitylation. We also find an uncanonical non-hydrophobic contact in the Bre1 RING-Rad6 interface, which positions Rad6 directly above the target H2B lysine residue. Our study provides mechanistic insights into the site-specific monoubiquitylation of H2B, reveals a critical role of nucleosomal DNA in mediating E3 ligase recognition, and provides a framework for understanding the cancer-driving mutations of RNF20/RNF40. | ||
- | + | ==See Also== | |
- | + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | |
- | + | *[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Current revision
RNF20-RNF40/hRad6A-Ub/nucleosome complex
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Categories: Homo sapiens | Large Structures | Ai H | Deng Z | Du Y | Liu L | Pan M | Sun M