Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins

Science

Volumn 275, Issue 5296, 1997, Pages 86-88

  Oliver, Jason D ^a   Van Der Wal, Fimme J ^a   Bulleid, Neil J ^a   High, Stephen ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE LINKED OLIGOSACCHARIDE; CALNEXIN; CALRETICULIN; CHAPERONE; GLYCOPROTEIN; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DOG; ENDOPLASMIC RETICULUM; GLYCOPROTEIN SYNTHESIS; MICROSOME; NONHUMAN; PANCREAS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CROSS LINKING; PROTEIN FOLDING; PROTEIN GLYCOSYLATION; PROTEIN PROTEIN INTERACTION; QUALITY CONTROL;

ANIMALS; CALCIUM-BINDING PROTEINS; CALNEXIN; CALRETICULIN; DOGS; ENDOPLASMIC RETICULUM; ENZYME INHIBITORS; FUNGAL PROTEINS; GLUCOSE; GLUCOSIDASES; GLYCOPROTEINS; GLYCOSYLATION; HEAT-SHOCK PROTEINS; INDOLIZINES; ISOMERASES; MICROSOMES; MOLECULAR WEIGHT; OXIDOREDUCTASES; PANCREAS; PROLACTIN; PROTEIN PRECURSORS; RIBONUCLEOPROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 0031035644     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.275.5296.86     Document Type: Article

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15. Antisera recognizing ERp57, the heavy chainbinding protein (BiP), and a 55-kD ER calciumbinding protein (ERG-55) were tested. Of these, only ERp57 was found to be cross-linked to PL62.CHO and no cross-linking products with PL62.Con were detected.
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17. ERp57 is also known as GRP58, ERp61, ER-60, Q-2, and HIP-70 [C. F. Bennett, J. M. Balcarek, A. Varrichio, S. T. Crooke, Nature 334, 268 (1988); S. P. Srivastava, N. Chen, Y. Liu, J. L. Holtzman, J. Biol. Chem. 266,20337 (1991); N. Hirano et al., Biochem. Biophys. Res. Commun. 204, 375 (1994)].
18. ERp57 is also known as GRP58, ERp61, ER-60, Q-2, and HIP-70 [C. F. Bennett, J. M. Balcarek, A. Varrichio, S. T. Crooke, Nature 334, 268 (1988); S. P. Srivastava, N. Chen, Y. Liu, J. L. Holtzman, J. Biol. Chem. 266,20337 (1991); N. Hirano et al., Biochem. Biophys. Res. Commun. 204, 375 (1994)].
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23. 2-terminal amino acid sequencing. The purified protein was then used to raise a rabbit polyclonal antibody. The resulting anti-ERp57 only functions for immunoprecipitation after SDS denaturation (Fig. 1B); thus, a reciprocal coimmunoprecipitation experiment (Fig. 2B) using anti-ERp57 in the first round was not possible.
24. After import of S. cerevisiae prepro-α factor cDNA (in pGEM) into microsomes, the resulting protein has three sites for N-linked glycosylation and nine lysine residues from which cross-linking may occur. Human IFN-γ has two sites for N-linked glycosylation, one cysteine residue, and 20 lysine residues. The transcription vector used was as described [N. J. Bulleid, E. Curling, R,B. Freedman, N. Jenkins, Biochem. J. 268, 777 (1990)].
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29. 2, and 50 mM Hepes-KOH (pH 7.9)], which permits the oxidation of full-length prolactin, and the samples were treated with puromycin for 5 min. SMCC was added to a final concentration of 1 mM from a 50 mM stock in DMSO; samples were incubated for 10 min and then quenched by addition of 0.1 volumes of 50 mM 2-mercaptoethanol and 500 mM glycine. All reactions were carried out at the translation temperature of 26°C.
30. Rabbit antibodies to canine ERp57 were purified from crude serum by affinity purification using protein immobilized on nitrocellulose [E. Harlow and D. Lane, Antibodies: A Laboratory Manual (Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1988)].
31. All of the glycosylated forms indicated in Fig. 3D were sensitive to digestion with endoglycosidase H. After import, signal sequence cleavage, and glycosylation, the major forms of PPα and IFN-γ had apparent molecular masses of 29 and 25 kD, respectively.
32. Supported by grants from the UK Biotechnology and Biological Sciences Research Council (BBSRC), the Human Frontier Science Program Organization (HFSPO), and the UK Medical Research Council. S.H. is a BBSRC Advanced Research Fellow. N.J.B. is a Royal Society Research Fellow. We thank C. Iwahashi for assistance with construct preparation, A. Helenius and members of his laboratory for advice and reagents, C. Stirling for S. cerevisiae prepro-α factor cDNA, J. L. Holtzman for anti-ERp57 (Q-2) serum, and several other groups that provided antisera to ER proteins.