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TDRD3 Is an Effector Molecule for Arginine-Methylated Histone Marks
Open accessAbstract
Summary Specific sites of histone tail methylation are associated with transcriptional activity at gene loci. These methyl-marks are interpreted by effector molecules, which harbor protein domains that bind the methylated motifs and facilitate either active or inactive states of transcription. CARM1 and PRMT1 are transcriptional coactivators that deposit H3R17me2a and H4R3me2a marks, respectively. We used a protein domain microarray approach to identify the tudor domain-containing protein TDRD3 as a “reader” of these marks. Importantly, TDRD3 itself is a transcriptional coactivator. This coactivator activity requires an intact tudor domain. TDRD3 is recruited to an estrogen responsive element in a CARM1-dependent manner. Furthermore, ChIP-seq analysis of TDRD3 reveals that it is predominantly localized to transcriptional start sites. Thus, TDRD3 is an effector molecule that promotes transcription by binding methylarginine marks on histone tails.
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Cites
Protein lysine methyltransferase G9a acts on non-histone targets
Rathert, P., Dhayalan, A., Murakami, M., Zhang, X., Tamas, R., Jurkowska, R., Komatsu, Y., Shinkai, Y., Cheng, X., & Jeltsch, A. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.88 · Cited by 347
Cited by
Histone methylation: a dynamic mark in health, disease and inheritance
Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241
Protein arginine methyltransferases and cancer
Yang, Y., & Bedford, M. T. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3409 · Cited by 1,083
Self-citationPerceiving the epigenetic landscape through histone readers
Musselman, C. A., Lalonde, M.-E., Côté, J., & Kutateladze, T. G. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2436 · Cited by 833
Brd4 and JMJD6-Associated Anti-Pause Enhancers in Regulation of Transcriptional Pause Release
Liu, W., Ma, Q., Wong, K., Li, W., Ohgi, K., Zhang, J., Aggarwal, A. K., & Rosenfeld, M. G. (2013) · Cell · doi:10.1016/j.cell.2013.10.056 · Cited by 406
Quantitative Proteomic Analysis of Histone Modifications
Huang, H., Lin, S., Garcia, B. A., & Zhao, Y. (2015) · Chemical Reviews · doi:10.1021/cr500491u · Cited by 370
Metadata
- Authors
- Yang, Y., Lu, Y., Espejo, A., Wu, J., Xu, W., Liang, S., & Bedford, M. T.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2010-12
- Volume
- 40
- Issue
- 6
- Pages
- 1016-1023
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2026081838
- Cited by
- 241
- References
- 1
- FWCI
- 7.09
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Yang, Y., Lu, Y., Espejo, A., Wu, J., Xu, W., Liang, S., & Bedford, M. T. (2010). TDRD3 Is an Effector Molecule for Arginine-Methylated Histone Marks. Molecular Cell. https://doi.org/10.1016/j.molcel.2010.11.024
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