Histones are the most abundant proteins bound to DNA in eukaryotic
cells. Post-translational modifications of histones, such as methylation,
acetylation and ubiquitination, influence accessibility to
DNA of factors involved in DNA damage repair and transcription. Monoubiquitination
of histone H2B at lysine 120 (H2Bub1) leads to physical separation of chromatin
strands and active recruitment of factors involved in histone cross-talk,
transcription and repair of DNA damage. Monoubiquitination is controlled by E3
ubiquitin ligases and deubiquitinases (DUBs). Both BRCA1 and the ring finger
protein RNF20 are H2Bub1-associated E3 ubiquitin ligases. Given the known involvement
of BRCA1 in high grade serous cancer (HGSC), this study aimed to determine the
influence of BRCA1 mutation and RNF20 levels on H2Bub1 in this malignancy.
We investigated a large HGSC patient cohort using immunohistochemistry to
determine global tumour levels of H2Bub1 and RNF20, and analysed the
association of H2Bub1 levels with germ-line BRCA1 mutation
status. Additionally, we used HGSC cell line models to determine the
relationship between BRCA1 expression, RNF20 and H2Bub1. GlobalH2Bub1was
lost in over 70% of HGSC. No significant correlation was observed between
germ-line BRCA1 mutation status or RNF20 levels and H2Bub1;
however, manipulation of BRCA1 and RNF20 expression in HGSC cell line models influenced
global H2Bub1 levels. H2Bub1 regulation is complex, appearing to rely on
multiple enzymatic processes. Targeting H2Bub1 may pose an attractive strategy
for the development of epigenetic based therapies for HGSC.