In:
eLife, eLife Sciences Publications, Ltd, Vol. 8 ( 2019-06-18)
Kurzfassung:
The SNF2h remodeler slides nucleosomes most efficiently as a dimer, yet how the two protomers avoid a tug-of-war is unclear. Furthermore, SNF2h couples histone octamer deformation to nucleosome sliding, but the underlying structural basis remains unknown. Here we present cryo-EM structures of SNF2h-nucleosome complexes with ADP-BeFx that capture two potential reaction intermediates. In one structure, histone residues near the dyad and in the H2A-H2B acidic patch, distal to the active SNF2h protomer, appear disordered. The disordered acidic patch is expected to inhibit the second SNF2h protomer, while disorder near the dyad is expected to promote DNA translocation. The other structure doesn’t show octamer deformation, but surprisingly shows a 2 bp translocation. FRET studies indicate that ADP-BeFx predisposes SNF2h-nucleosome complexes for an elemental translocation step. We propose a model for allosteric control through the nucleosome, where one SNF2h protomer promotes asymmetric octamer deformation to inhibit the second protomer, while stimulating directional DNA translocation.
Materialart:
Online-Ressource
ISSN:
2050-084X
DOI:
10.7554/eLife.46057.001
DOI:
10.7554/eLife.46057.002
DOI:
10.7554/eLife.46057.003
DOI:
10.7554/eLife.46057.004
DOI:
10.7554/eLife.46057.005
DOI:
10.7554/eLife.46057.006
DOI:
10.7554/eLife.46057.007
DOI:
10.7554/eLife.46057.008
DOI:
10.7554/eLife.46057.009
DOI:
10.7554/eLife.46057.010
DOI:
10.7554/eLife.46057.011
DOI:
10.7554/eLife.46057.012
DOI:
10.7554/eLife.46057.013
DOI:
10.7554/eLife.46057.014
DOI:
10.7554/eLife.46057.022
DOI:
10.7554/eLife.46057.015
DOI:
10.7554/eLife.46057.016
DOI:
10.7554/eLife.46057.017
DOI:
10.7554/eLife.46057.018
DOI:
10.7554/eLife.46057.019
DOI:
10.7554/eLife.46057.020
DOI:
10.7554/eLife.46057.021
DOI:
10.7554/eLife.46057.023
DOI:
10.7554/eLife.46057.024
DOI:
10.7554/eLife.46057.025
DOI:
10.7554/eLife.46057.026
DOI:
10.7554/eLife.46057.027
DOI:
10.7554/eLife.46057.029
DOI:
10.7554/eLife.46057.030
DOI:
10.7554/eLife.46057.045
DOI:
10.7554/eLife.46057.046
Sprache:
Englisch
Verlag:
eLife Sciences Publications, Ltd
Publikationsdatum:
2019
ZDB Id:
2687154-3