Fig. 4

Segments influencing oligomer assembly and functionality. a Diagram of CPN60 subunits and the constructed chaperonin chimeras of CPN60s. Domain designation and amino acid numbering were used with respect to GroEL. E1 domain (1–137), I1 domain (138–190), A (191–374), I2 (375–409), E2 (410–548). b Solubility and oligomeric states of chaperonin chimeras. Whole cell lysate (WC) from 1 mL of induced cells were resolved with 12 % SDS-PAGE. The soluble fractions were separated with 12 % SDS PAGE and 6 % native PAGE. Purified CPN60α monomer, CPN60β1 oligomer, and uninduced cell lysate (–) were loaded as controls. Proteins were visualized by Coomassie staining. The positions of oligomers and monomers are indicated by an arrow and *, respectively. c Oligomer formation and disassembly of chaperonin chimeras. The whole cell lysates (WC) were analyzed by 12 % SDS-PAGE, and soluble fractions (S) were resolved with 12 % SDS-PAGE and 6 % native PAGE with or without incubation for 30 min at 25 °C with 5 mM ATP/Mg. Purified CPN60α monomer, CPN60β1 oligomer, and CPN60β2 oligomer were loaded as controls. The oligomer and monomer positions are indicated by an arrow and *, respectively. Proteins were visualized by Coomassie staining