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Papers In Press, published online ahead of print April 20, 2000
Department of Medicinal Chemistry and Pharmacognosy, University of Illinois-Chicago College of Pharmacy, Chicago, IL 60607-7173
Corresponding Author: blond{at}uic.edu
The activity of HSP70 proteins is regulated by accessory proteins, among which the most studied are the members of the DnaJ-like protein family. BiP/GRP78 chaperones the translocation and maturation of secreted and membrane proteins in the endoplasmic reticulum. No DnaJ-like partner has been described so far to regulate the function of mammalian BiP/GRP78. We show here that murine BiP/GRP78 interacts with the lumenal J-domain of the murine transmembrane protein MTJ1 (J-MTJ1). J-MTJ1 stimulates the ATPase activity of BiP/GRP78 at stoichiometric concentrations. The C-terminal tail of BiP/GRP78 is not required for the interaction with J-MTJ1, leaving the function of this portion of the molecule still unclear. Physical interactions between J-MTJ1 and BiP/GRP78 are stable and can be abolished by a single histidine -> glutamine substitution in the highly conserved HPD motif shared by all DnaJ-like proteins. The J-MTJ1 fragment, but not the mutant J-MTJ1:H89Q stimulates the ATPase activity of E. coli DnaK, although at a higher concentration than its genuine partner DnaJ. Full-length DnaJ does not stimulate BiP over the range of concentrations investigated. These results indicate that the J domain of MTJ1 is sufficient for its interaction with BiP/GRP78 and cannot be substituted by the E. coli DnaJ.
J. Biol. Chem, 10.1074/jbc.M001333200
Submitted on February 17, 2000
Revised on April 18, 2000
Accepted on April 20, 2000
Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1
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