Chaperoning of the histone octamer by the acidic domain of DNA repair factor APLF

Ivan Corbeski, Xiaohu Guo, Bruna V Eckhardt, Domenico Fasci, Wouter Wiegant, Melissa A Graewert, Kees Vreeken, Hans Wienk, Dmitri I Svergun, Albert J R Heck, Haico van Attikum, Rolf Boelens, Titia K Sixma, Francesca Mattiroli, Hugo van Ingen

Research output: Contribution to journal/periodicalArticleScientificpeer-review

11 Citations (Scopus)


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 (APLFAD) can assemble the histone octamer in a single step and deposit it on DNA to form nucleosomes. The crystal structure of the APLFAD-histone octamer complex shows that APLFAD tethers the histones in their nucleosomal conformation. Mutations of key aromatic anchor residues in APLFAD 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.

Original languageEnglish
Pages (from-to)eabo0517
JournalScience advances
Issue number30
Publication statusPublished - 29 Jul 2022


  • DNA/chemistry
  • DNA Repair
  • Histone Chaperones/genetics
  • Histones/metabolism
  • Molecular Chaperones/genetics
  • Nucleosomes


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