A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase

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...

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Bibliographic Details
Published in:	Cell cycle (Georgetown, Tex.) Vol. 11; no. 13; pp. 2538 - 2544
Main Authors:	Gatti, Marco, Pinato, Sabrina, Maspero, Elena, Soffientini, Paolo, Polo, Simona, Penengo, Lorenza
Format:	Journal Article
Language:	English
Published:	United States Taylor & Francis 01.07.2012 Landes Bioscience
Subjects:	Amino Acid Sequence Binding Biology Bioscience Calcium Cancer Cell Chromatin Assembly and Disassembly chromatin remodeling Cycle DNA damage response DNA Repair DNA-Binding Proteins - metabolism epigenetics HEK293 Cells histone ubiquitination Histones - chemistry Histones - genetics Histones - metabolism Humans Landes Molecular Sequence Data Mutation Organogenesis Protein Structure, Tertiary Proteins RNF168 ubiquitin ligase Ubiquitin-Protein Ligases - metabolism Ubiquitination
ISSN:	1538-4101, 1551-4005, 1551-4005
Online Access:	Get full text
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