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J Biol Chem, Vol. 274, Issue 40, 28083-28086, October 1, 1999
From the Department of Biochemistry, Kansas State University,
Manhattan, Kansas 66506
ClpB is a heat-shock protein from
Escherichia coli with an unknown function. We studied a
possible molecular chaperone activity of ClpB in vitro.
Firefly luciferase was denatured in urea and then diluted into the
refolding buffer (in the presence of 5 mM ATP and 0.1 mg/ml
bovine serum albumin). Spontaneous reactivation of luciferase was very
weak (less than 0.02% of the native activity) because of extensive
aggregation. Conventional chaperone systems (GroEL/GroES and
DnaK/DnaJ/GrpE) or ClpB alone did not reactivate luciferase under those
conditions. However, ClpB together with DnaK/DnaJ/GrpE greatly enhanced
the luciferase activity regain (up to 57% of native activity) by
suppressing luciferase aggregation. This coordinated function of ClpB
and DnaK/DnaJ/GrpE required ATP hydrolysis, although the ClpB ATPase
was not activated by native or denatured luciferase. When the
chaperones were added to the luciferase refolding solutions after 5-25
min of refolding, ClpB and DnaK/DnaJ/GrpE recovered the luciferase
activity from preformed aggregates. Thus, we have identified a
novel multi-chaperone system from E. coli, which is
analogous to the Hsp104/Ssa1/Ydj1 system from yeast. ClpB is the only
known bacterial Hsp100 protein capable of cooperating with other
heat-shock proteins in suppressing and reversing protein aggregation.
COMMUNICATION
ClpB Cooperates with DnaK, DnaJ, and GrpE in Suppressing Protein
Aggregation
A NOVEL MULTI-CHAPERONE SYSTEM FROM ESCHERICHIA
COLI
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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