Oligomerization properties of ERp29, an endoplasmic reticulum stress protein

Funding Information: This work was supported by the Swedish Medical Research Council. We thank Prof. H.F. Gilbert for helpful discussions and critical reading of the manuscript. Copyright: Copyright 2007 Elsevier B.V., All rights reserved. Correction(s) for this article: Oligomerization properties of ERp29, an endoplasmic reticulum stress protein. FEBS Letters,Vol.433, N.3, p.335-335. - First Published online: June 28, 1999.ERp29, a novel and ubiquitously expressed endoplasmic reticulum (ER) stress-inducible protein, was recently isolated and cDNA cloned in our laboratory. Using size exclusion chromatography and chemical cross-linking we have assessed the oligomerization properties of ERp29. Purified ERp29 in solution as well as in rat hepatoma cells self-associates predominantly into homodimers. Labeling of the cells with [35S]methionine with subsequent cross-linking and immunprecipitation showed that ERp29 interacts with a number of ER proteins, one of which was previously identified as BiP/GRP78. Secondary structure prediction and fold recognition methods indicate that the native conformation of ERp29 resembles the thioredoxin fold, a structural motif characteristic of a number of enzymes with the redox function, including protein disulfide isomerase (with which ERp29 shares limited sequence similarity). Dimerization of the protein is suggested to be advantageous for the protein binding potential of ERp29.publishersversionPeer reviewe