Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones.
Genes Dev
; 35(23-24): 1610-1624, 2021 12 01.
Article
em En
| MEDLINE
| ID: mdl-34819355
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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Histonas
/
Chaperonas de Histonas
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article