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J Biol Chem, Vol. 274, Issue 29, 20110-20115, July 16, 1999
From the Howard Hughes Medical Institute and Department of Cell
Biology, Harvard Medical School, Boston, Massachusetts 02115
Proteins of the Hsp70 family of ATPases interact
with a conserved domain of their J-protein partners, the J-domain, to
function in numerous cellular processes. We have studied the
interaction of BiP, an Hsp70 family member in the lumen of the
endoplasmic reticulum, with the J-domain of Sec63p, a component of the
Sec complex involved in post-translational protein translocation across the endoplasmic reticulum membrane. In a real-time solid phase binding
assay, BiP binds to the immobilized Sec complex or to a fusion protein
of the J-domain and glutathione S-transferase in a reaction
that requires ATP hydrolysis. In the final complex, BiP is bound in the
ADP form with its peptide binding pocket occupied. An intact peptide
binding pocket is required for this interaction. Our experiments
suggest that the activation of BiP by the J-domain involves a transient
contact between these components, and that in the absence of
physiological substrates, J-activated BiP binds even to the J-proteins themselves.
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