FEBS Letters | |
Cdc48 can distinguish between native and non‐native proteins in the absence of cofactors | |
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
【 预 览 】
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