Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides
Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides
The AAA+ chaperone ClpB solubilizes in cooperation with the DnaK chaperone system aggregated proteins. The mechanistic features of the protein disaggregation process are poorly understood. Here, we investigated the mechanism of ClpB/DnaK-dependent solubilization of heat-aggregated malate dehydrogenase (MDH) by following characteristics of MDH aggregates during the disaggregation reaction. We demonstrate that disaggregation is achieved by the continuous extraction of unfolded MDH molecules and not by fragmentation of large MDH aggregates. These findings support a ClpB-dependent threading mechanism as an integral part of the disaggregation reaction.
AAA+ protein, Chaperone, ClpB, DnaK, Protein disaggregation
351-356
Schlieker, Christian
46637f9a-380e-48ff-a5de-053afea81fb2
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Bukau, Bernd
a8504059-3987-4f2a-b1e9-34504b602fb4
Mogk, Axel
592acbce-9fcf-4273-9ba8-45026c857e2f
17 December 2004
Schlieker, Christian
46637f9a-380e-48ff-a5de-053afea81fb2
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Bukau, Bernd
a8504059-3987-4f2a-b1e9-34504b602fb4
Mogk, Axel
592acbce-9fcf-4273-9ba8-45026c857e2f
Schlieker, Christian, Tews, Ivo, Bukau, Bernd and Mogk, Axel
(2004)
Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides.
FEBS Letters, 578 (3), .
(doi:10.1016/j.febslet.2004.11.051).
Abstract
The AAA+ chaperone ClpB solubilizes in cooperation with the DnaK chaperone system aggregated proteins. The mechanistic features of the protein disaggregation process are poorly understood. Here, we investigated the mechanism of ClpB/DnaK-dependent solubilization of heat-aggregated malate dehydrogenase (MDH) by following characteristics of MDH aggregates during the disaggregation reaction. We demonstrate that disaggregation is achieved by the continuous extraction of unfolded MDH molecules and not by fragmentation of large MDH aggregates. These findings support a ClpB-dependent threading mechanism as an integral part of the disaggregation reaction.
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Published date: 17 December 2004
Keywords:
AAA+ protein, Chaperone, ClpB, DnaK, Protein disaggregation
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Local EPrints ID: 500825
URI: http://eprints.soton.ac.uk/id/eprint/500825
ISSN: 0014-5793
PURE UUID: 128c236a-fbed-4c10-88ee-68b75ea11908
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Date deposited: 13 May 2025 17:20
Last modified: 14 May 2025 01:44
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Contributors
Author:
Christian Schlieker
Author:
Bernd Bukau
Author:
Axel Mogk
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