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Functional crosstalk between histone H2B ubiquitylation and H2A modifications and variants
Felix Wojcik1, Geoffrey P Dann1,2, Leslie Y Beh1,3,4
1Department of Chemistry, Princeton University, Princeton, NJ, 08544, USA.
Nature Communications
|April 13, 2018
Summary
Histone H2B ubiquitylation (H2BK120ub) is crucial for active genes. This study reveals that pre-existing modifications on histone H2A tails regulate H2BK120ub deposition, impacting gene transcription.
Area of Science:
- Epigenetics and chromatin biology
- Molecular mechanisms of gene regulation
- Histone posttranslational modifications
Background:
- Histone H2B ubiquitylation at lysine 120 (H2BK120ub) is a key epigenetic mark linked to active transcription.
- While H2BK120ub influences chromatin structure and downstream modifications, its regulatory mechanisms, especially concerning substrate modification status, remain unclear.
Purpose of the Study:
- To investigate how pre-existing chromatin modifications affect the de novo ubiquitylation of histone H2B at K120.
- To identify the specific histone modifications that regulate the E2:E3 ligase pair UBE2A:RNF20/40 activity.
Main Methods:
- Utilized an unbiased library screening approach to profile the impact of various histone PTMs.
- Conducted biochemical assays and cell-based studies to validate findings.
- Focused on the human E2:E3 ligase pair UBE2A:RNF20/40.
Main Results:
- H2BK120ub deposition is highly sensitive to posttranslational modifications (PTMs) on the N-terminal tail of histone H2A.
- This regulatory crosstalk was also observed for the histone variant H2A.Z.
- Demonstrated that H2A PTMs influence the spatial organization of H2BK120ub on gene bodies.
Conclusions:
- Crosstalk between histone H2A PTMs and H2B ubiquitylation is a critical regulatory mechanism.
- This crosstalk influences the localization of H2BK120ub, thereby impacting transcriptional regulation.
- Highlights a novel layer of epigenetic control over gene expression.
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