Is it a wrap? Nucleosome interactions of the BRCA1-binding partner, BARD1, steal the scene

• Published in: Nature structural & molecular biology Vol. 28; no. 9; pp. 708 - 710
• Main Author: Morris, Joanna R.
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.09.2021; Nature Publishing Group
• Subjects: 631/337/1427/2190; 631/80/458/582; Analysis; Ankyrin Repeat; Biochemistry; Biological Microscopy; Biomedical and Life Sciences; BRCA1 protein; BRCA1 Protein - metabolism; Breast cancer; Cancer; Chromatin; Core particles; Coronaviruses; Cryoelectron Microscopy; DNA Damage; DNA repair; Fanconi Anemia Complementation Group N Protein - metabolism; Genetic aspects; Histone Code; Histone H2A; Histones - metabolism; Humans; Hydrogen bonds; Life Sciences; Membrane Biology; Molecular biology; Mutagenesis; Mutation; Mutation, Missense; Neoplasm Proteins - metabolism; Neoplasms - enzymology; News & Views; news-and-views; Nucleosomes - metabolism; Phthalazines - pharmacology; Piperazines - pharmacology; Protein Binding; Protein Domains; Protein Structure; Recombinational DNA Repair; RNA polymerase; Tumor Suppressor Proteins - chemistry; Tumor Suppressor Proteins - genetics; Tumor Suppressor Proteins - metabolism; Ubiquitin; Ubiquitin-conjugating enzyme; Ubiquitin-Protein Ligases - chemistry; Ubiquitin-Protein Ligases - genetics; Ubiquitin-Protein Ligases - metabolism; Ubiquitination; United Kingdom
• ISSN: 1545-9993; 1545-9985
• DOI: 10.1038/s41594-021-00658-7

Emerging findings provide compelling evidence that the BRCA1-binding partner BARD1 contributes yet further to BRCA1 function. BARD1 is crucial for positioning the E2 ubiquitin-conjugating enzyme that confers specificity of its ligase to residues on histone H2A, and BARD1 also promotes DNA damage–induced chromatin recruitment through an interaction with ubiquitin-conjugated Lys13 or Lys15 of H2A on the nucleosome core particle.