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J Biol Chem, Vol. 274, Issue 27, 19316-19322, July 2, 1999
From the ClpA, a member of the Clp/Hsp100 family of
ATPases, is both an ATP-dependent molecular chaperone and
the regulatory component of ClpAP protease. We demonstrate that
chaperone and protease activities occur concurrently in ClpAP complexes
during a single round of RepA binding to ClpAP and
ATP-dependent release. This result was substantiated with a
ClpA mutant, ClpA(K220V), carrying an amino acid substitution in the
N-terminal ATP binding site. ClpA(K220V) is unable to activate RepA,
but the presence of ClpP or chemically inactivated ClpP restores its
ability to activate RepA. The presence of ClpP simultaneously
facilitates degradation of RepA. ClpP must remain bound to ClpA(K220V)
for these effects, indicating that both chaperone and proteolytic
activities of the mutant complex occur concurrently. ClpA(K220V) itself
is able to form stable complexes with RepA in the presence of a poorly hydrolyzed ATP analog, adenosine 5'-O-(thiotriphosphate),
and to release RepA upon exchange of adenosine
5'-O-(thiotriphosphate) with ATP. However, the released
RepA is inactive in DNA binding, indicating that the N-terminal ATP
binding site is essential for the chaperone activity of ClpA. Taken
together, these results suggest that substrates bound to the complex of
the proteolytic and ATPase components can be partitioned between
release/reactivation and translocation/degradation.
Concurrent Chaperone and Protease Activities of ClpAP and the
Requirement for the N-terminal ClpA ATP Binding Site for Chaperone
Activity
,,
Laboratory of Molecular Biology and
§ Laboratory of Cell Biology, National Cancer Institute,
National Institutes of Health, Bethesda, Maryland 20892
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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