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. 2023 Jan 5;24(2):1051. doi: 10.3390/ijms24021051

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© 2023 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Functional Domains of histone chaperones involved in transcription, replacement and DNA repair. Each diagram displays a scaled representation of the domain structure for SPT6 (A), SWR1 (B), SWC2 (C), APLF (D), histone chaperones from Physarum, yeast, human and Arabidopsis. Diagrams for XRCC1 (E) display a scaled representation of this protein from Physarum, yeast, human, Xenopus, D. rerio and Arabidopsis. Human possesses two SWR1 orthologues named Hs-p400 and HsSCRAP. Each domain is depicted at its position by a different color and the code is indicated at the right. Names of domains involved in histone binding are in bold and underlined. HtH, Helix-turn-Helix; HhH, Helix-hairpin-Helix; HHH, HHH domain 9; S1, S1 RNA-binding domain; SH2, Src-homology 2 domain; WG/GW, domain containing Glycin (G) and Tryptophan (W) repeats; HSA, Helicase/SANT-associated; SANT, Swi3/Ada2/N-Cor/TFIIIB; polyQ, poly-glutamine domain; FHA, ForkHead-Associated; PBZ, PolyADP-ribose-Binding Zinc-finger; BRCT, BRCA1 C-terminal.