Structure and dynamics of the yeast SWR1-nucleosome complex.

Oliver Willhoft, Mohamed Ghoneim, Chia-Liang Lin, Eugene Y D Chua, Martin Wilkinson, Yuriy Chaban, Rafael Ayala, Elizabeth A McCormack, Lorraine Ocloo, David S Rueda, Dale B Wigley

Science (New York, N.Y.) 2018 Oct 12

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The yeast SWR1 complex exchanges histone H2A in nucleosomes with Htz1 (H2A.Z in humans). The cryo-electron microscopy structure of the SWR1 complex bound to a nucleosome at 3.6-angstrom resolution reveals details of the intricate interactions between components of the SWR1 complex and its nucleosome substrate. Interactions between the Swr1 motor domains and the DNA wrap at superhelical location 2 distort the DNA, causing a bulge with concomitant translocation of the DNA by one base pair, coupled to conformational changes of the histone core. Furthermore, partial unwrapping of the DNA from the histone core takes place upon binding of nucleosomes to SWR1 complex. The unwrapping, as monitored by single-molecule data, is stabilized and has its dynamics altered by adenosine triphosphate binding but does not require hydrolysis. Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.

Citation

Oliver Willhoft, Mohamed Ghoneim, Chia-Liang Lin, Eugene Y D Chua, Martin Wilkinson, Yuriy Chaban, Rafael Ayala, Elizabeth A McCormack, Lorraine Ocloo, David S Rueda, Dale B Wigley. Structure and dynamics of the yeast SWR1-nucleosome complex. Science (New York, N.Y.). 2018 Oct 12;362(6411)