Rxivist logo

Rxivist combines preprints from bioRxiv with data from Twitter to help you find the papers being discussed in your field. Currently indexing 55,243 bioRxiv papers from 254,840 authors.

Electron cryo-microscopy structures of remodeler-nucleosome intermediates suggest allosteric control through the nucleosome.

By Jean-Paul Armache, Nathan Gamarra, Stephanie L Johnson, John D. Leonard, Shenping Wu, Geeta J. Narlikar, Yifan Cheng

Posted 15 Feb 2019
bioRxiv DOI: 10.1101/550970

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 reaction intermediates. In one structure, histone residues near the dyad and in the H2A-H2B acidic patch, distal to the active SNF2h protomer, are disordered. The disordered acidic patch is expected to inhibit the second SNF2h promoter, while disorder near the dyad is expected to promote DNA translocation. The other structure doesn't show octamer deformation, but surprisingly shows a 2bp 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.

Download data

  • Downloaded 901 times
  • Download rankings, all-time:
    • Site-wide: 7,051 out of 55,243
    • In biophysics: 206 out of 2,330
  • Year to date:
    • Site-wide: 939 out of 55,243
  • Since beginning of last month:
    • Site-wide: 3,536 out of 55,243

Altmetric data


Downloads over time

Distribution of downloads per paper, site-wide


Sign up for the Rxivist weekly newsletter! (Click here for more details.)


News