Abstract:
:The HIRA histone chaperone complex deposits the histone variant H3.3 onto chromatin in a DNA synthesis-independent manner. It comprises three identified subunits, HIRA, UBN1 and CABIN1, however the functional oligomerization state of the complex has not been investigated. Here we use biochemical and crystallographic analysis to show that the HIRA subunit forms a stable homotrimer that binds two subunits of CABIN1 in vitro. A HIRA mutant that is defective in homotrimer formation interacts less efficiently with CABIN1, is not enriched at DNA damage sites upon UV irradiation and cannot rescue new H3.3 deposition in HIRA knockout cells. The structural homology with the homotrimeric replisome component Ctf4/AND-1 enables the drawing of parallels and discussion of the functional importance of the homotrimerization state of the HIRA subunit.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Ray-Gallet D,Ricketts MD,Sato Y,Gupta K,Boyarchuk E,Senda T,Marmorstein R,Almouzni Gdoi
10.1038/s41467-018-05581-ysubject
Has Abstractpub_date
2018-08-06 00:00:00pages
3103issue
1issn
2041-1723pii
10.1038/s41467-018-05581-yjournal_volume
9pub_type
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