7V6Q

Crystal structure of sNASP-ASF1A-H3.1-H4 complex

Summary for 7V6Q

• Entry DOI: 10.2210/pdb7v6q/pdb
• Related: 7V6P
• Descriptor: Histone chaperone ASF1A, Histone H3.1, Histone H4, ... (7 entities in total)
• Functional Keywords: histone chaperone, chaperone
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 8
• Total formula weight: 153967.69

Authors

Liu, C.P.,Xu, R.M. (deposition date: 2021-08-20, release date: 2021-12-29, Last modification date: 2023-11-29)

Primary citation

Liu, C.P.,Jin, W.,Hu, J.,Wang, M.,Chen, J.,Li, G.,Xu, R.M.
Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones.
Genes Dev., 35:1610-1624, 2021

PubMed Abstract: Chromosomal duplication requires de novo assembly of nucleosomes from newly synthesized histones, and the process involves a dynamic network of interactions between histones and histone chaperones. sNASP and ASF1 are two major histone H3-H4 chaperones found in distinct and common complexes, yet how sNASP binds H3-H4 in the presence and absence of ASF1 remains unclear. Here we show that, in the presence of ASF1, sNASP principally recognizes a partially unfolded Nα region of histone H3, and in the absence of ASF1, an additional sNASP binding site becomes available in the core domain of the H3-H4 complex. Our study also implicates a critical role of the C-terminal tail of H4 in the transfer of H3-H4 between sNASP and ASF1 and the coiled-coil domain of sNASP in nucleosome assembly. These findings provide mechanistic insights into coordinated histone binding and transfer by histone chaperones.

PubMed: 34819355
DOI: 10.1101/gad.349100.121

Experimental method

X-RAY DIFFRACTION (3 Å)