Structure and dynamics of the yeast SWR1-nucleosome complex | Zendy

Oliver Willhöft | Zendy; Mohamed Ghoneim | Zendy; ChiaLiang Lin | Zendy; Eugene Chua | Zendy; Martin Wilkinson | Zendy; Yuriy Chaban | Zendy; Rafael Ayala | Zendy; Elizabeth A. McCormack | Zendy; Lorraine Ocloo | Zendy; David Rueda | Zendy; Dale B. Wigley | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Structure and dynamics of the yeast SWR1-nucleosome complex

Author(s) -

Oliver Willhöft,

Mohamed Ghoneim,

ChiaLiang Lin,

Eugene Chua,

Martin Wilkinson,

Yuriy Chaban,

Rafael Ayala,

Elizabeth A. McCormack,

Lorraine Ocloo,

David Rueda,

Dale B. Wigley

Publication year - 2018

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aat7716

Subject(s) - nucleosome , histone octamer , histone , biophysics , dna , linker dna , chemistry , microbiology and biotechnology , biology , biochemistry

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research