Structural insight into BRCA1-BARD1 complex recruitment to damaged chromatin.

The BRCA1-BARD1 complex directs the DNA double-strand break (DSB) repair pathway choice to error-free homologous recombination (HR) during the S-G2 stages. Targeting BRCA1-BARD1 to DSB-proximal sites requires BARD1-mediated nucleosome interaction and histone mark recognition. Here, we report the cryo-EM structure of BARD1 bound to a ubiquitinated nucleosome core particle (NCP) at 3.

Recognition of the inherently unstable H2A nucleosome by Swc2 is a major determinant for unidirectional H2A.Z exchange.

The multisubunit chromatin remodeler SWR1/SRCAP/p400 replaces the nucleosomal H2A-H2B dimer with the free-form H2A.Z-H2B dimer, but the mechanism governing the unidirectional H2A-to-H2A.Z exchange remains elusive.

Structural basis of nucleosome dynamics modulation by histone variants H2A.B and H2A.Z.2.2.

Nucleosomes are dynamic entities with wide-ranging compositional variations. Human histone variants H2A.B and H2A.

Role of a DEF/Y motif in histone H2A-H2B recognition and nucleosome editing.

The SWR complex edits the histone composition of nucleosomes at promoters to facilitate transcription by replacing the two nucleosomal H2A-H2B (A-B) dimers with H2A.Z-H2B (Z-B) dimers. Swc5, a subunit of SWR, binds to A-B dimers, but its role in the histone replacement reaction was unclear.

NMR investigations on H2A-H2B heterodimer dynamics conferred by histone variant H2A.Z.

H2A.Z, a highly conserved histone H2A variant in eukaryotes, plays critical roles in multiple nuclear events. H2A.

Crystal structure of the histone heterodimer containing histone variant H2A.Bbd.

H2A.Bbd, the most divergent histone variant among all known H2A type histones, is involved in gene transcription, spermiogenesis, DNA replication and RNA splicing. Incorporation of H2A.

Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z.

H2A.Z is a highly conserved histone variant in all species. The chromatin deposition of H2A.