Oligomerization properties of ERp29, an endoplasmic reticulum stress protein

FEBS Letters

Baryshev, Mikhail³  Mkrtchiana, Souren²  Sandalova, Tatyana¹  Sharipo, Anatoly³  Schneider, Gunter¹  Ingelman-Sundberg, Magnus²  Matvijenko, Olga³ 

[1] Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77 Stockholm, Sweden;Division of Molecular Toxicology, Institute of Environmental Medicine, Karolinska Institute, P.O. Box 201, S-171 77 Stockholm, Sweden;Laboratory of Applied Microbiology, Kirchenshtein Institute of Microbiology and Virology, LV-1067 Riga, Latvia

关键词: ERp29;    Protein disulfide isomerase;    Molecular chaperone;    Cross-linking;    Size exclusion chromatography;    Oligomer;    ER;    endoplasmic reticulum;    PDI;    protein disulfide isomerase;    PMSF;    phenylmethylsulfonyl fluoride;   

DOI  :  10.1016/S0014-5793(98)00786-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 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.

【 授权许可】

Unknown