BRCA1 Is a Histone-H2A-Specific Ubiquitin Ligase

Kalb, Reinhard; Mallery, Donna L.; Larkin, Conor; Huang, Jeffrey T. J.; Hiom, Kevin

doi:10.1016/j.celrep.2014.07.025

Datensatz

DATENSATZ AKTIONENEXPORT

Zur Ablage hinzufügen

Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben

Zeitschriftenartikel

BRCA1 Is a Histone-H2A-Specific Ubiquitin Ligase

MPG-Autoren

/persons/resource/persons132143

Kalb, Reinhard
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

Externe Ressourcen

Es sind keine externen Ressourcen hinterlegt

Volltexte (beschränkter Zugriff)

Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.

Volltexte (frei zugänglich)

1-s2.0-S2211124714006093-main.pdf
(beliebiger Volltext), 910KB

Ergänzendes Material (frei zugänglich)

Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar

Zitation

Kalb, R., Mallery, D. L., Larkin, C., Huang, J. T. J., & Hiom, K. (2014). BRCA1 Is a Histone-H2A-Specific Ubiquitin Ligase. CELL REPORTS, 8(4), 999-1005. doi:10.1016/j.celrep.2014.07.025.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0023-FD15-5

Zusammenfassung

The RING domain proteins BRCA1 and BARD1 comprise a heterodimeric ubiquitin (E3) ligase that is required for the accumulation of ubiquitin conjugates at sites of DNA damage and for silencing at DNA satellite repeat regions. Despite its links to chromatin, the substrate and underlying function of the BRCA1/BARD1 ubiquitin ligase remain unclear. Here, we show that BRCA1/BARD1 specifically ubiquitylates histone H2A in its C-terminal tail on lysines 127 and 129 in vitro and in vivo. The specificity for K127-129 is acquired only when H2A is within a nucleosomal context. Moreover, site-specific targeting of the BRCA1/BARD1 RING domains to chromatin is sufficient for H2Aub foci formation in vivo. Our data establish BRCA1/BARD1 as a histone-H2A-specific E3 ligase, helping to explain its localization and activities on chromatin in cells.