To slide or not to slide: key role of the hexasome in chromatin remodeling revealed

• Published in: Nature structural & molecular biology Vol. 31; no. 5; pp. 742 - 746
• Main Author: Rhodes, Daniela
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.05.2024; Nature Publishing Group
• Subjects: 631/337/100; 631/337/100/102; 631/337/100/1701; 631/535/1258/1259; Binding sites; Biochemistry; Biological Microscopy; Biomedical and Life Sciences; Chromatin Assembly and Disassembly; Chromatin remodeling; Cryoelectron Microscopy; Deoxyribonucleic acid; DNA; DNA - chemistry; DNA - metabolism; Genomes; Histone H2A; Histones; Histones - chemistry; Histones - metabolism; Humans; Life Sciences; Membrane Biology; Microscopy; Models, Molecular; Molecular biology; Nucleosomes; Nucleosomes - chemistry; Nucleosomes - metabolism; Nucleosomes - ultrastructure; Perspective; Protein Structure; RNA polymerase; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - metabolism; Substrates
• ISSN: 1545-9993; 1545-9985; 1545-9985
• DOI: 10.1038/s41594-024-01278-7

Hexasomes are non-canonical nucleosomes that package DNA with six instead of eight histones. First discovered 40 years ago as a consequence of transcription, two near-atomic-resolution cryo-EM structures of the hexasome in complex with the chromatin remodeler INO80 have now started to unravel its mechanistic impact on the regulatory landscape of chromatin. Loss of one histone H2A–H2B dimer converts inactive nucleosomes into distinct and favorable substrates for ATP-dependent chromatin remodeling. Hexasomes are non-canonical nucleosomes that package DNA with six instead of eight histones. Here, the author contextualizes two recent studies on the interplay of the chromatin remodeler INO80 with hexasomes with historical literature on the subject.