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Originally published In Press as doi:10.1074/jbc.M001333200 on April 20, 2000

J. Biol. Chem., Vol. 275, Issue 26, 19620-19627, June 30, 2000
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Interaction of Murine BiP/GRP78 with the DnaJ Homologue MTJ1*

Mathieu Chevalier, Hong Rhee, Ebrahim C. ElguindiDagger , and Sylvie Y. Blond§

From the Department of Medicinal Chemistry and Pharmacognosy, University of Illinois, Chicago, Illinois 60607-7173

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 right-arrow 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 fragment, stimulates the ATPase activity of Escherichia 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 E. coli DnaJ.

* This work was supported in part by National Institutes of Health Grant GM58107 (to S. Y. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by a grant from the Talaat Basha Family Foundation.

§ To whom correspondence should be addressed: Center for Pharmaceutical Biotechnology (M/C 870), College of Pharmacy, Dept. of Medicinal Chemistry and Pharmacognosy, Molecular Biology Research Bldg., University of Illinois, 900 S. Ashland Ave., Chicago, IL 60607-7173. Tel.: 312-996-5416; Fax: 312-413-9303; E-mail: blond@uic.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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