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J. Biol. Chem., Vol. 281, Issue 44, 33727-33738, November 3, 2006

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ERp27, a New Non-catalytic Endoplasmic Reticulum-located Human Protein Disulfide Isomerase Family Member, Interacts with ERp57^*

Heli I. Alanen, Richard A. Williamson, Mark J. Howard, Feras S. Hatahet, Kirsi E. H. Salo, Annika Kauppila, Sakari Kellokumpu, and Lloyd W. Ruddock¹

From the Department of Biochemistry and Biocenter Oulu, University of Oulu, P. O. Box 3000, FIN-90014, Finland and the Department of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, United Kingdom

Protein folding and quality control in the endoplasmic reticulum are critical processes for which our current understanding is far from complete. Here we describe the functional characterization of a new human 27.7-kDa protein (ERp27). We show that ERp27 is a two-domain protein located in the endoplasmic reticulum that is homologous to the non-catalytic b and b' domains of protein disulfide isomerase. ERp27 was shown to bind -somatostatin, the standard test peptide for protein disulfide isomerase-substrate binding, and this ability was localized to the second domain of ERp27. An alignment of human ERp27 and human protein disulfide isomerase allowed for the putative identification of the peptide binding site of ERp27 indicating conservation of the location of the primary substrate binding site within the protein disulfide isomerase family. NMR studies revealed a significant conformational change in the b'-like domain of ERp27 upon substrate binding, which was not just localized to the substrate binding site. In addition, we report that ERp27 is bound by ERp57 both in vitro and in vivo by a similar mechanism by which ERp57 binds calreticulin.

Received for publication, May 5, 2006 , and in revised form, July 14, 2006.

^* The work was supported by Biocenter Oulu, the University of Oulu, the Sigrid Juselius Foundation, and the Wellcome Trust (UK). 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.

¹ To whom correspondence should be addressed. Tel.: 358-8-553-1683; Fax: 358-8-553-1141; E-mail: Lloyd.ruddock{at}oulu.fi.

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