Cdc48 can distinguish between native and non‐native proteins in the absence of cofactors

FEBS Letters

Thoms, Sven¹ 

[1] ZMBH, Center for Molecular Biology, Heidelberg University, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany

关键词: Cdc48;    p97;    VCP;    ATPase associated with various cellular activities;    Chaperone;    Ubiquitin;    ER-associated protein;    Hsp70;   

DOI  :  10.1016/S0014-5793(02)02777-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The ATPase Cdc48 is required for membrane fusion and protein degradation. Recently it has been suggested that Cdc48 in a complex with Ufd1 and Npl4 acts as an ubiquitin-dependent chaperone. Here it is shown that recombinant Cdc48 alone can distinguish between the native and the non-native conformation of model substrates. First, Cdc48 prevents luciferase from aggregating following a heat shock. Second, it inhibits the aggregation of rhodanese upon dilution. Third, Cdc48 binds specifically to heat-denatured luciferase. These chaperone-like functions seem to be independent of ATPase activity. Furthermore, Cdc48 can act as a co-chaperone in the Hsc70–Hsp40 chaperone system. These results show that Cdc48 possesses chaperone-like activities and can functionally interact with Hsc70. Cdc48's ability to recognise denatured proteins can also be a source of unspecific binding in biochemical interaction experiments.

【 授权许可】

Unknown