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J Biol Chem, Vol. 273, Issue 45, 29475-29480, November 6, 1998
,
From the The folding of protein structures often requires
the presence of molecular chaperones and/or chaperonin complexes. We
here investigated the inhibitory effects of the chaperone cofactors Hop/p60 and Hap46. By coimmunoprecipitation, we observed a direct interaction of the eukaryotic chaperonin-containing TCP-1 (CCT) purified from rabbit reticulocyte lysate with Hop/p60. By contrast, Hap46 was not coprecipitated. Binding of Hop/p60 to CCT is dependent on
the presence of ATP or ADP and occurs through carboxyl-terminal sequences of Hop/p60. Hop/p60 significantly stimulates nucleotide exchange on CCT but not its ATPase activity, while Hap46 has no effects. We used denatured firefly luciferase as a model protein and
found decreased binding to CCT in the presence of Hop/p60 and ATP. This
coincides with the inhibitory effect of Hop/p60 on luciferase
reactivation in an assay using purified CCT in combination with hsc70
and hsp40. We also observed that an antibody directed against one of
the subunits of CCT efficiently inhibits refolding in a system which
depends on crude reticulocyte lysate.
Universität Heidelberg,
Biochemie-Zentrum Heidelberg, Biologische Chemie, Im Neuenheimer Feld
501, D-69120 Heidelberg, Germany and § Laboratoire de
Enzymologie et Biochimie Structurales, Centre National de la Recherche
Scientifique, Bat. 34-Avenue de la Terrasse,
F-91198 Gif-sur-Yvette, France
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