Chaperoning of the histone octamer by the acidic domain of DNA repair factor APLF.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 35895815.
- Also identified by DOI 10.1126/sciadv.abo0517 and PMC identifier 9328677.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Nucleosome assembly requires the coordinated deposition of histone complexes H3-H4 and H2A-H2B to form a histone octamer on DNA. In the current paradigm, specific histone chaperones guide the deposition of first H3-H4 and then H2A-H2B. Here, we show that the acidic domain of DNA repair factor APLF (APLF<sup>AD</sup>) can assemble the histone octamer in a single step and deposit it on DNA to form nucleosomes. The crystal structure of the APLF<sup>AD</sup>-histone octamer complex shows that APLF<sup>AD</sup> tethers the histones in their nucleosomal conformation. Mutations of key aromatic anchor residues in APLF<sup>AD</sup> affect chaperone activity in vitro and in cells. Together, we propose that chaperoning of the histone octamer is a mechanism for histone chaperone function at sites where chromatin is temporarily disrupted.
Medical subject headings
- Histones
- Nucleosomes