Poly‐L‐lysine enhances the protein disaggregation activity of ClpB

FEBS Letters

Schlieker, Christian²  Mogk, Axel²  Strub, Christine¹  Bukau, Bernd² 

[1] Institut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Str. 7, D-79104 Freiburg, Germany;ZMBH, Universität Heidelberg, Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany

关键词: Protein disaggregation;    Chaperone;    ClpB;    DnaK;    AAA+ protein;   

DOI  :  10.1016/S0014-5793(03)00985-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The Hsp100 protein ClpB is a member of the AAA+ protein family that mediates the solubilization of aggregated proteins in cooperation with the DnaK chaperone system. Unstructured polypeptides such as casein or poly-L-lysine have been shown to stimulate the ATPase activity of ClpB and thus may both act as substrates. Here we compared the effects of α-casein and poly-L-lysine on the ATPase and chaperone activities of ClpB. α-Casein stimulated ATP hydrolysis by both AAA domains of ClpB and inhibited the ClpB-dependent solubilization of aggregated proteins if present in excess. In contrast, poly-L-lysine stimulated exclusively the ATPase activity of the second AAA domain and increased the disaggregation activity of ClpB. Thus poly-L-lysine does not act as substrate, but rather represents an effector molecule, which enhances the chaperone activity of ClpB.

【 授权许可】

Unknown