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Oligomerization properties of ERp29, an endoplasmic reticulum stress protein
Author(s) -
Mkrtchiana Souren,
Baryshev Mikhail,
Matvijenko Olga,
Sharipo Anatoly,
Sandalova Tatyana,
Schneider Gunter,
Ingelman-Sundberg Magnus
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00786-8
Subject(s) - endoplasmic reticulum , protein disulfide isomerase , unfolded protein response , biochemistry , immunoprecipitation , chemistry , thioredoxin , chaperone (clinical) , enzyme , complementary dna , isomerase , biology , microbiology and biotechnology , gene , medicine , pathology
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 [ 35 S]methionine with subsequent cross‐linking and immunoprecipitation 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.