Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Thoms Sdoi
10.1016/s0014-5793(02)02777-1keywords:
subject
Has Abstractpub_date
2002-06-05 00:00:00pages
107-10issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302027771journal_volume
520pub_type
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