2021
DOI: 10.1101/2021.12.24.474097
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Chaperoning of the histone octamer by the acidic domain of DNA repair factor APLF

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(1-5). 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 … Show more

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“…Experimental structural biology would be required to confirm these models. The ability of a peptide to act as a chaperone for an intact histone octamer has been observed before for the APLF peptide (28,30). The MIER1:octamer complex would appear to allow initial binding of DNA to the H3:H4 dyad position.…”
Section: Discussionmentioning
confidence: 69%
“…Experimental structural biology would be required to confirm these models. The ability of a peptide to act as a chaperone for an intact histone octamer has been observed before for the APLF peptide (28,30). The MIER1:octamer complex would appear to allow initial binding of DNA to the H3:H4 dyad position.…”
Section: Discussionmentioning
confidence: 69%