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Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides
Author(s) -
Schlieker Christian,
Tews Ivo,
Bukau Bernd,
Mogk Axel
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.11.051
Subject(s) - clpb , chaperone (clinical) , solubilization , malate dehydrogenase , protein aggregation , chemistry , biochemistry , biophysics , threading (protein sequence) , biology , enzyme , heat shock protein , protein structure , medicine , pathology , gene
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.