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

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 Lett

journal_title

FEBS letters

authors

Thoms S

doi

10.1016/s0014-5793(02)02777-1

keywords:

subject

Has Abstract

pub_date

2002-06-05 00:00:00

pages

107-10

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579302027771

journal_volume

520

pub_type

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