Binding of Hsp17 proteins to liposomes made of total polar lipids
isolated from heat-treated cells. A, purity of recombinant
proteins was assayed by SDS-PAGE and revealed by Coomassie blue staining. Low
molecular weight markers (LMW) display protein bands referring to
molecular masses of 94, 67, 43, 30, 20, and 14 kDa, respectively. B,
purified proteins were incubated with liposomes for 1 h and then fractionated
into lipid bound (pellet) and soluble (supernatant) fractions. The samples
were solubilized under reducing conditions and analyzed by SDS-PAGE and
Coomassie blue staining. C, the binding assay was repeated with
vesicles made of 14C-labeled lipids. The arrow indicates
the band corresponding to the Hsp17 associated with 14C-labeled
lipids. Lipid content of the pelleted Q16R Hsp17 fraction solubilized under
reducing conditions was revealed by fluorography.