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Volume 272, Number 50, Issue of December 12, 1997
pp. 31420-31426
(Received for publication, June 16, 1997, and in revised form, August 29, 1997)
From The Physiological Laboratory, Liverpool University,
P.O. Box 147, Crown Street,
Liverpool L69 3BX, United Kingdom
The "J" domains of eukaryotic DnaJ-like
proteins specify interaction with various Hsp70s. The conserved
tripeptide, HPD, present in all J domains has been shown to be
important for the interaction between yeast and bacterial DnaJ/Hsp70
protein pairs. We have characterized mutations in the HPD motif of the
synaptic vesicle protein cysteine-string protein (Csp). Mutation of the
histidine (H43Q) or aspartic acid (D45A) residues of this motif reduced the ability of Csp to stimulate the ATPase activity of mammalian Hsc70.
The H43Q and D45A mutant proteins were not able to stimulate the ATPase
activity of Hsc70 to any significant extent. The mutant proteins were
characterized by competition assays, tryptic digestion analysis, and
direct binding analysis from which it was seen that these proteins were
defective in binding to Hsc70. Thus, the HPD motif of Csp is required
for binding to Hsc70. We also analyzed the interaction between Csp and
a model substrate protein, denatured firefly luciferase. Both Csp1 and
the C-terminally truncated isoform Csp2 were able to prevent
aggregation of heat-denatured luciferase, and they also cooperated with
Hsc70 to prevent aggregation. In addition, complexes of Csp1 or Csp2
with Hsc70 and luciferase were isolated, confirming that these proteins
interact and that Csps can bind directly to denatured proteins. Csp1
and Csp2 isoforms must differ in some aspect other than interaction
with Hsc70 and substrate protein. These results show that both Csp1 and
Csp2 can bind a partially unfolded protein and act as chaperones. This suggests that Csps may have a general chaperone function in regulated exocytosis.
The Molecular Chaperone Function of the Secretory Vesicle
Cysteine String Proteins
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