tailieunhanh - Báo cáo khoa học: Dimerization and oligomerization of the chaperone calreticulin

The chaperone calreticulin is a highly conserved eukaryotic protein mainly located in the endoplasmic reticulum. It contains a free cysteine SH group but does not form disul-fide-bridged dimers under physiological conditions,indica-ting that the SH group may not be fully accessible in the native protein. Using PAGE,urea gradient gel electro-phoresis,capillary electrophoresis and MS,we show that dimerization through the SH group can be induced by lowering the pH to 5–6,heating,or under conditions that favour partial unfolding such as urea concentrations above SDS concentrations above . . | Eur. J. Biochem. 270 414 414 s 2003 FEBS 2003 doi Dimerization and oligomerization of the chaperone calreticulin Charlotte S. Jorgensen1. L Rebekka Rvder1 Anne Steino1. Peter HoiruD2. Jesner Hansen2 N. Helena Bever3. B MB B Niels Hb Hb Heegaard3 and Gunnar Houen1 1 Department of Research and Development Statens Serum Institut Copenhagen Denmark 2Department of Biochemistry and Molecular Biology University of Southern Denmark Odense Denmark 3Department of Autoimmunology Statens Serum Institut Copenhagen Denmark The chaperone calreticulin is a highly conserved eukaryotic protein mainly located in the endoplasmic reticulum. It contains a free cysteine SH group but does not form disulfide-bridged dimers under physiological conditions indicating that the SH group may not be fully accessible in the native protein. Using PAGE urea gradient gel elec_ tro-phoresis capillay c etrophoresis nnd MS. we show that dimerization through the SH group can be induced by lowering the pH to 5-6 haniing. or undec condoiont that favour partial unfolding such as urea concentrations above M or SDS concentrations above . Moreover we show that calreticulin also has the ability to self-oligomerize through noncovalent interactions at urea concentrations above M at pH below or above pH 10 at rempera-tures above 40 C or m die presence of 11 igh concentrations of organic solvents 25 renditiens tiiat lSrtotll jiM- ial unfolding or an intramolecular local conformational change that allows oligomerization resulting in a heterogeneous mixture of oligomers consisting of up to 10 calreticulin monomers. The oligomeric calreticulin was very stable but oligomerization was partially reversed by addition of 8 M urea or 1 SDS and heat-induced oligomerization could be inhibited by 8 M urea or 1 SDS when present during heating. Comparison of the binding properties of monomeric and oligomeric calreticulin in solid-phase assays showed increased binding to peptides

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