Histone H2B Mutations in Cancer
نویسندگان
چکیده
منابع مشابه
Histone H2B ubiquitination: the cancer connection.
Post-translational modifications of histones play a critical role in gene expression control. Ultimately, cancer is a disease of aberrant gene expression. Accordingly, several histone-modifying enzymes have been described as proto-oncogenes or tumor suppressors. Recent reports, including one from Shema and colleagues (pp. 2664- 2676) in the October 1, 2008, issue of Genes and Development, indic...
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Covalent modification of histones by ubiquitylation is a prominent epigenetic mark that features in a variety of chromatin-based events such as histone methylation, gene silencing, and repair of DNA damage. The prototypical example of histone ubiquitylation is that of histone H2B in Saccharomyces cerevisiae. In this case, attachment of ubiquitin to lysine 123 (K123) of H2B is important for regu...
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The reiterated nature of histone genes has hampered genetic approach to dissect the role of histones in chromatin dynamics. We here report isolation of three temperature-sensitive (ts) Schizosaccharomyces pombe strains, containing amino-acid substitutions in the sole histone H2B gene (htb1+). The mutation sites reside in the highly conserved, non-helical residues of H2B, which are implicated in...
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The trans-histone regulatory cross talk between H2BK123 ubiquitination (H2Bub1) and H3K4 and H3K79 methylation is not fully understood. In this study, we report that the residues arginine 119 and threonine 122 in the H2B C-terminal helix are important for transcription and cell growth and play a direct role in controlling H2Bub1 and H3K4 methylation. These residues modulate H2Bub1 levels by con...
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Histone H2B O-GlcNAcylation is an important post-translational modification of chromatin during gene transcription. However, how this epigenetic modification is regulated remains unclear. Here we found that the energy-sensing adenosine-monophosphate-activated protein kinase (AMPK) could suppress histone H2B O-GlcNAcylation. AMPK directly phosphorylates O-linked β-N-acetylglucosamine (O-GlcNAc) ...
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ژورنال
عنوان ژورنال: Biomedicines
سال: 2021
ISSN: 2227-9059
DOI: 10.3390/biomedicines9060694