Oligomerization properties of ERp29, an endoplasmic reticulum stress protein

Souren Mkrtchiana, Mikhail Baryshev, Olga Matvijenko, Anatoly Sharipo, Tatyana Sandalova, Gunter Schneider, Magnus Ingelman-Sundberg

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)
5 Downloads (Pure)


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.

Original languageEnglish
Pages (from-to)322-326
Number of pages5
JournalFEBS Letters
Issue number3
Publication statusPublished - 24 Jul 1998


  • Cross-linking
  • ERp29
  • Molecular chaperone
  • Oligomer
  • Protein disulfide isomerase
  • Size exclusion chromatography

Field of Science*

  • 1.6 Biological sciences

Publication Type*

  • 1.1. Scientific article indexed in Web of Science and/or Scopus database


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