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J. Biol. Chem., Vol. 279, Issue 18, 18277-18287, April 30, 2004
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**
From the
Institute of Biochemistry and Institute of Molecular Biology and Biophysics, ETH Zurich, CH-8093 Zurich, Switzerland, ¶School of Pharmacy, University of Connecticut, Storrs, Connecticut 06269, and ||Boston Biomedical Research Institute, Watertown, Massachusetts 02472
The thiol-disulfide oxidoreductase ERp57 is a soluble protein of the endoplasmic reticulum and the closest known homologue of protein disulfide isomerase. The protein interacts with the two lectin chaperones calnexin and calreticulin and thereby promotes the oxidative folding of newly synthesized glycoproteins. Here we have characterized several fundamental structural and functional properties of ERp57 in vitro, such as the domain organization, shape, redox potential, and the ability to catalyze different thiol-disulfide exchange reactions. Like protein disulfide isomerase, we find ERp57 to be comprised of four structural domains. The protein has an elongated shape of 3.4 ± 0.1 nm in diameter and 16.8 ± 0.5 nm in length. The two redox-active a and a' domains were determined to have redox potentials of –0.167 and –0.156 V, respectively. Furthermore, ERp57 was shown to efficiently catalyze disulfide reduction, disulfide isomerization, and dithiol oxidation in substrate proteins. The implications of these findings for the function of the protein in vivo are discussed.
Received for publication, December 23, 2003 , and in revised form, February 10, 2004.
Note Added in Proof—During the revision of this manuscript, articles by Pollock et al. and Russell et al. (Pollock, S., Kozlov, G., Pelletier, M.-F., Trempe, J.-F., Jansen, G., Sitnikov, D., Bergeron, J. J. M., Gehring, K., Ekiel, I., and Thomas, D. Y. (2004) EMBO J. 23, 1020–1029 and Russell, S., Ruddock, L. W., Salo, E. E. H., Oliver, J. D., Roebuck, Q. P., Llewellyn, D. H., Roderick, H. L., Koivunen, P., Myllyharju, J., and High, S. (February 10, 2004) J. Biol. Chem. 10.1074/jbc.M400575200) have mapped the binding site for calreticulin and calnexin in ERp57, whereas an article by Silvennoinen et al. (Silvennoinen, L., Myllyharju, J., Ruoppolo, M., Orru, S., Caterino, M., Kivrikko, K. I., and Koivunen, P. (2004) J. Biol. Chem. 279, 13607–13615) has also identified four thioredoxin-like domains in ERp57.
* This work was supported by grants from the Swiss National Research Foundation (to A. H. and L. E.), the ETH Zürich (to A. H. and L. E.), the NCCR structural biology program (to P. F. and R. G.), by NIAID Grant AI45070 from the National Institutes of Health (to M. B.), and in part by National Science Foundation Grant BIR-9513060 (to W. F. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
** To whom all correspondence should be addressed. Tel.: 41-1-632-3003; Fax: 41-1-632-1269; E-mail: lars.ellgaard{at}bc.biol.ethz.ch.
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