Publication: A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase
A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase
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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, 11, 2538–2544. https://doi.org/10.4161/cc.20919
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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 ligas
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- Gatti, Marco
- Pinato, Sabrina
- Maspero, Elena
- Soffientini, Paolo
- Polo, Simona
- Penengo, Lorenza
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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, 11, 2538–2544. https://doi.org/10.4161/cc.20919
