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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Characterization of pancreatic ERj3p, ahomolog of yeast DnaJ-like protein Scj1p

C. Bies / R. Blum / J. Dudek / W. Nastainczyk / S. Oberhauser / M. Jung / R. Zimmermann

Citation Information: Biological Chemistry. Volume 385, Issue 5, Pages 389–395, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2004.043, June 2005

Publication History:
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We have previously identified in the human EST sequence data base four overlapping clones that could be aligned with both a predicted protein sequence, deduced from the C. elegans genomic sequence, and partial amino acid sequences, obtained for a protein from canine pancreatic microsomes. We suggested that these proteins are homologs of yeast microsomal and DnaJlike protein Scj1p and termed them ERj3p. Here we verified the predicted protein sequence of human ERj3p by sequence analysis of the corresponding cDNA. Multiple alignment of related sequences identified these proteins as true homologs of yeast Scj1p. Biochemical analysis of the canine protein characterized ERj3p as a soluble glycoprotein of the pancreatic endoplasmic reticulum. This pancreatic DnaJ-like protein was shown to interact with lumenal DnaK-like proteins, such as BiP. Furthermore, we found that ERj3p interacts with SDF2L1 protein that may be involved in protein O-glycosylation. We propose that ERj3p represents a cochaperone of DnaKlike chaperones of the mammalian endoplasmic reticulum and is involved in folding and maturation of newly synthesized proteins.

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