PARP1 and CBP lose their footing in cancer

The human histone macroH2A.1.1 recruits activated PARP1 enzyme to chromatin through its poly(ADP-ribose)-binding macrodomain. New work shows that PARP1 and CBP can be displaced from chromatin in cancer cells that have lost macroH2A.1.1, thus leading to changes in histone H2B acetylation at cancer-re...

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Veröffentlicht in:	Nature structural & molecular biology 2014-11, Vol.21 (11), p.947-948
Hauptverfasser:	Timinszky, Gyula, Ladurner, Andreas G
Format:	Artikel
Sprache:	eng
Schlagworte:	631/337/100/2285 631/337/100/2286 631/67 Binding sites Biochemistry Biological Microscopy Cancer Enzymes Gene Expression Regulation, Neoplastic Genes Genetic aspects Health aspects Histones - genetics Humans Life Sciences Membrane Biology news-and-views Peptide Fragments - genetics Physiological aspects Poly (ADP-Ribose) Polymerase-1 Poly(ADP-ribose) Polymerases - genetics Protein Structure Sialoglycoproteins - genetics Transcription, Genetic
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Zusammenfassung:	The human histone macroH2A.1.1 recruits activated PARP1 enzyme to chromatin through its poly(ADP-ribose)-binding macrodomain. New work shows that PARP1 and CBP can be displaced from chromatin in cancer cells that have lost macroH2A.1.1, thus leading to changes in histone H2B acetylation at cancer-relevant genes.
ISSN:	1545-9993 1545-9985
DOI:	10.1038/nsmb.2913