5YJE

Crystal structure of HIRA(644-1017)

Summary for 5YJE

• Entry DOI: 10.2210/pdb5yje/pdb
• Descriptor: Protein HIRA, SULFATE ION (3 entities in total)
• Functional Keywords: histone chaperone, gene regulation
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 3
• Total formula weight: 126241.23

Authors

Sato, Y.,Senda, M.,Senda, T. (deposition date: 2017-10-10, release date: 2018-06-20, Last modification date: 2024-03-27)

Primary citation

Ray-Gallet, D.,Ricketts, M.D.,Sato, Y.,Gupta, K.,Boyarchuk, E.,Senda, T.,Marmorstein, R.,Almouzni, G.
Functional activity of the H3.3 histone chaperone complex HIRA requires trimerization of the HIRA subunit
Nat Commun, 9:3103-3103, 2018

PubMed 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.

PubMed: 30082790
DOI: 10.1038/s41467-018-05581-y

Experimental method

X-RAY DIFFRACTION (2.45 Å)