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Published on: January 26, 2018
TDRD3 is an effector molecule for arginine-methylated histone marks
Yanzhong Yang1, Yue Lu, Alexsandra Espejo
1The University of Texas MD Anderson Cancer Center, Science Park-Research Division, P.O. Box 389, Smithville, TX 78957, USA.
Molecular Cell
|December 22, 2010
Summary
Tudor domain-containing protein TDRD3 reads histone methylation marks, acting as a transcriptional coactivator. TDRD3 binds these marks to promote gene transcription, highlighting its role in gene regulation.
Area of Science:
- Molecular Biology
- Epigenetics
- Gene Regulation
Background:
- Histone tail methylation is crucial for transcriptional regulation.
- Specific methyl marks are recognized by effector proteins.
- CARM1 and PRMT1 deposit key histone methylation marks.
Purpose of the Study:
- To identify effector molecules that read histone methylation marks.
- To characterize the role of TDRD3 in transcriptional regulation.
Main Methods:
- Protein domain microarray to identify "readers" of histone marks.
- Chromatin immunoprecipitation sequencing (ChIP-seq) to determine TDRD3 localization.
- Functional assays to assess TDRD3 coactivator activity.
Main Results:
- TDRD3 identified as a "reader" of H3R17me2a and H4R3me2a marks via its Tudor domain.
- TDRD3 functions as a transcriptional coactivator.
- TDRD3 is recruited to target genes in a CARM1-dependent manner.
- ChIP-seq shows TDRD3 enrichment at transcriptional start sites.
Conclusions:
- TDRD3 is a novel effector molecule that promotes transcription.
- TDRD3's coactivator function depends on its Tudor domain.
- TDRD3 links histone methylation marks to transcriptional activation.
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