Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation

Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation

The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation with the Hsp70 system. Essential for disaggregation, the ClpB middle domain (MD) is a coiled-coil propeller that binds Hsp70. Although the ClpB subunit structure is known, positioning of the MD in the hexamer and its me...

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Bibliographic Details
Main Authors: Marta Carroni, Eva Kummer, Yuki Oguchi, Petra Wendler, Daniel K Clare, Irmgard Sinning, Jürgen Kopp, Axel Mogk, Bernd Bukau, Helen R Saibil
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2014-04-01
Series:eLife
Subjects:
single particle EM
ClpB/Hsp104
protein unfolding
Online Access:https://elifesciences.org/articles/02481

Internet

https://elifesciences.org/articles/02481

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