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Published on: August 15, 2014
Histone deimination antagonizes arginine methylation
Graeme L Cuthbert1, Sylvain Daujat, Andrew W Snowden
1Gurdon Institute and Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QR, United Kingdom.
Cell
|September 2, 2004
Summary
Histone arginine deimination by peptidyl arginine deiminase 4 (PADI4) antagonizes active transcription by preventing arginine methylation. This novel deimination process represses gene induction, offering new insights into epigenetic regulation.
Area of Science:
- Epigenetics
- Molecular Biology
- Gene Regulation
Background:
- Histone arginine methylation is associated with active gene transcription.
- CARM1 methyltransferase is recruited to promoters like pS2 for transcriptional activation.
- A process that antagonizes methylation, called deimination, is introduced.
Purpose of the Study:
- To investigate the role of deimination in gene regulation.
- To identify the enzyme responsible for histone arginine deimination.
- To determine if deimination antagonizes arginine methylation and affects transcription.
Main Methods:
- Characterization of peptidyl arginine deiminase 4 (PADI4) activity on histone H3.
- Assessing the effect of PADI4 deimination on CARM1-mediated arginine methylation.
- In vivo promoter targeting experiments to evaluate PADI4's repressive role.
Main Results:
- PADI4 specifically deiminates arginine residues R2, R8, R17, and R26 in the histone H3 tail.
- Deimination by PADI4 prevents arginine methylation by CARM1.
- PADI4 represses hormone receptor-mediated gene induction and is recruited to downregulated promoters.
Conclusions:
- Deimination is a novel epigenetic mechanism that antagonizes transcriptional activation mediated by histone arginine methylation.
- PADI4-mediated deimination plays a repressive role in gene regulation.
- Understanding deimination provides new targets for therapeutic intervention in diseases involving aberrant gene expression.
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