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. 2014 Sep 15;1:12. doi: 10.3389/fmolb.2014.00012

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Copyright © 2014 Sousa.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Proposed mechanisms of ClpB/Hsp104 mediated protein disaggregation. (A) Threading: The ClpB/Hsp104 hexamer engages a protein in an aggregate and pulls it through its central pore to separate it from the aggregate. (B) Deoligomerization: A ClpB/Hsp104 hexamer binds an aggregate and then deoligomerizes so that each ClpB/Hsp104 protomer pulls a single bound protein away from the aggregate. (C) Crowbar: The mobile M-domains of the ClpB/Hsp104 hexamer engage and break up the aggregate.