The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase
Open accessAbstract
Ubiquitination of histones plays a critical role in the regulation of several processes within the nucleus, including maintenance of genome stability and transcriptional regulation. The only known ubiquitination site on histones is represented by a conserved Lys residue located at the C terminus of the protein. Here, we describe a novel ubiquitin mark at the N-terminal tail of histone H2As consisting of two Lys residues at positions 13 and 15 (K13/K15). This "bidentate" site is a target of the DNA damage response (DDR) ubiquitin ligases RNF8 and RNF168. Histone mutants lacking the K13/K15 site impair RNF168- and DNA damage-dependent ubiquitination. Conversely, inactivation of the canonical C-terminal site prevents the constitutive monoubiquitination of histone H2As but does not abolish the ubiquitination induced by RNF168. A ubiquitination-defective mutant is obtained by inactivating both the N- and the C-terminal sites, suggesting that these are unique, non-redundant acceptors of ubiquitination on histone H2As. This unprecedented result implies that RNF168 generates a qualitatively different Ub mark on chromatin.
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Cites
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
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
Histones: annotating chromatin
Campos, E. I., & Reinberg, D. (2009) · Annual Review of Genetics · doi:10.1146/annurev.genet.032608.103928 · Cited by 852
Abraxas and RAP80 Form a BRCA1 Protein Complex Required for the DNA Damage Response
Wang, B., Matsuoka, S., Ballif, B. A., Zhang, D., Smogorzewska, A., Gygi, S. P., & Elledge, S. J. (2007) · Science · doi:10.1126/science.1139476 · Cited by 695
Cited by
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark
Fradet-Turcotte, A., Canny, M. D., Escribano-Díaz, C., Orthwein, A., Leung, C. C. Y., Huang, H., Landry, M.-C., Kitevski-LeBlanc, J., Noordermeer, S. M., Sicheri, F., et al. (2013) · Nature · doi:10.1038/nature12318 · Cited by 686
Regulation of DNA Damage Responses by Ubiquitin and SUMO
Jackson, S. P., & Durocher, D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.017 · Cited by 601
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
Gruosso, T., Mieulet, V., Cardon, M., Bourachot, B., Kieffer, Y., Devun, F., Dubois, T., Dutreix, M., Vincent‐Salomon, A., Miller, K. M., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201505891 · Cited by 179
Metadata
- Authors
- Gatti, M., Pinato, S., Maspero, E., Soffientini, P., Polo, S., & Penengo, L.
- Venue
- Cell Cycle
- Publisher
- Informa UK Limited
- Published
- 2012-07
- Volume
- 11
- Issue
- 13
- Pages
- 2538-2544
- ISSN
- 1538-4101 (ISSN-L)
- 1551-4005
- OpenAlex
- W2171955018
- Cited by
- 168
- References
- 4
- FWCI
- 6.27
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Gatti, M., Pinato, S., Maspero, E., Soffientini, P., Polo, S., & Penengo, L. (2012). A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase. Cell Cycle. https://doi.org/10.4161/cc.20919
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