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Cryo-EM structures of remodeler-nucleosome intermediates suggest allosteric control through the nucleosome


ABSTRACT:

SUBMITTER: Jean-Paul Armache 

PROVIDER: EMPIAR-10287 | biostudies-other |

REPOSITORIES: biostudies-other

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Cryo-EM structures of remodeler-nucleosome intermediates suggest allosteric control through the nucleosome.

Armache Jean Paul JP   Gamarra Nathan N   Johnson Stephanie L SL   Leonard John D JD   Wu Shenping S   Narlikar Geeta J GJ   Cheng Yifan Y  

eLife 20190618


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-BeF<sub>x</sub> 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  ...[more]

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