The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A
Abstract
Biological responses to histone methylation critically depend on the faithful readout and transduction of the methyl-lysine signal by “effector” proteins, yet our understanding of methyl-lysine recognition has so far been limited to the study of histone binding by chromodomain and WD40-repeat proteins. The double tudor domain of JMJD2A, a Jmjc domain–containing histone demethylase, binds methylated histone H3-K4 and H4-K20. We found that the double tudor domain has an interdigitated structure, and the unusual fold is required for its ability to bind methylated histone tails. The cocrystal structure of the JMJD2A double tudor domain with a trimethylated H3-K4 peptide reveals that the trimethyl-K4 is bound in a cage of three aromatic residues, two of which are from the tudor-2 motif, whereas the binding specificity is determined by side-chain interactions involving amino acids from the tudor-1 motif. Our study provides mechanistic insights into recognition of methylated histone tails by tudor domains and reveals the structural intricacy of methyl-lysine recognition by two closely spaced effector domains.
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Cites
Structure and ligand of a histone acetyltransferase bromodomain
Dhalluin, C., Carlson, J. E., Zeng, L., He, C., Aggarwal, A. K., Zhou, M.-M., & Zhou, M.-M. (1999) · Nature · doi:10.1038/20974 · Cited by 1,732
Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
Huyen, Y., Zgheib, O., DiTullio Jr, R. A., Gorgoulis, V. G., Zacharatos, P., Petty, T. J., Sheston, E. A., Mellert, H. S., Stavridi, E. S., & Halazonetis, T. D. (2004) · Nature · doi:10.1038/nature03114 · Cited by 884
Cited by
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
“…to chromatin, but in these instances the enzymatic activity resides within the methyl-binding protein: JMJD2A is a histone lysine demethylase that binds via a tudor domain and CHD1 is an ATPase that binds via a chromodomain (Huang et al., 2006; Pray-Grant et al., 2005; Sims et al., 2005).”
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
The complex language of chromatin regulation during transcription
Berger, S. L. (2007) · Nature · doi:10.1038/nature05915 · Cited by 2,768
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
JmjC-domain-containing proteins and histone demethylation
Klose, R. J., Kallin, E. M., & Zhang, Y. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1945 · Cited by 1,290
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Metadata
- Authors
- Huang, Y., Fang, J., Bedford, M. T., Zhang, Y., & Xu, R.-M.
- Venue
- Science
- Published
- 2006-05-05
- Volume
- 312
- Issue
- 5774
- Pages
- 748-751
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2144275955
- Cited by
- 446
- References
- 2
- FWCI
- 15.10
- Type
- journal article
- Language
- en
- Open access
- closed
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- Huang, Y., Fang, J., Bedford, M. T., Zhang, Y., & Xu, R.-M. (2006). Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A. Science. https://doi.org/10.1126/science.1125162
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