EMD-38860
structure of RSF-147bp NCP complex Class 0
EMD-38860
Single-particle6.08 Å
Deposition: 26/01/2024Map released: 03/07/2024
Last modified: 03/07/2024
Sample Organism:
Heardaxius
Sample: structure of RSF-147bp NCP complex Class 0
Deposition Authors: Zhang JL
Sample: structure of RSF-147bp NCP complex Class 0
Deposition Authors: Zhang JL
Cryo-EM structure and functional analysis of the chromatin remodeler RSF.
Zhang J,
Zhao H,
Zou B,
Li H,
Dong S,
Guan J,
Wang C,
Li W,
Liu Y,
Chen Y,
Rasheed N,
He J
(2024) Acta Crystallogr F Struct Biol Commun , 80 , 125 - 134
(2024) Acta Crystallogr F Struct Biol Commun , 80 , 125 - 134
Abstract:
The RSF complex belongs to the ISWI chromatin-remodeling family and is composed of two subunits: RSF1 (remodeling and spacing factor 1) and SNF2h (sucrose nonfermenting protein 2 homolog). The RSF complex participates in nucleosome spacing and assembly, and subsequently promotes nucleosome maturation. Although SNF2h has been extensively studied in the last few years, the structural and functional properties of the remodeler RSF1 still remain vague. Here, a cryo-EM structure of the RSF-nucleosome complex is reported. The 3D model shows a two-lobe architecture of RSF, and the structure of the RSF-nucleosome (flanked with linker DNA) complex shows that the RSF complex moves the DNA away from the histone octamer surface at the DNA-entry point. Additionally, a nucleosome-sliding assay and a restriction-enzyme accessibility assay show that the RSF1 subunit may cause changes in the chromatin-remodeling properties of SNF2h. As a `nucleosome ruler', the results of an RSF-dinucleosome binding affinity test led to the proposal that the critical distance that RSF `measures' between two nucleosomes is about 24 base pairs.
The RSF complex belongs to the ISWI chromatin-remodeling family and is composed of two subunits: RSF1 (remodeling and spacing factor 1) and SNF2h (sucrose nonfermenting protein 2 homolog). The RSF complex participates in nucleosome spacing and assembly, and subsequently promotes nucleosome maturation. Although SNF2h has been extensively studied in the last few years, the structural and functional properties of the remodeler RSF1 still remain vague. Here, a cryo-EM structure of the RSF-nucleosome complex is reported. The 3D model shows a two-lobe architecture of RSF, and the structure of the RSF-nucleosome (flanked with linker DNA) complex shows that the RSF complex moves the DNA away from the histone octamer surface at the DNA-entry point. Additionally, a nucleosome-sliding assay and a restriction-enzyme accessibility assay show that the RSF1 subunit may cause changes in the chromatin-remodeling properties of SNF2h. As a `nucleosome ruler', the results of an RSF-dinucleosome binding affinity test led to the proposal that the critical distance that RSF `measures' between two nucleosomes is about 24 base pairs.