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Fig. 1 | BMC Biology

Fig. 1

From: Structural insight into the cooperation of chloroplast chaperonin subunits

Fig. 1

Interaction of homo-oligomeric CPN60β1 with co-chaperonin. a Analytical gel filtration of CPN60β1-cochaperonin complexes. A 50-μL reaction mixture containing 2 μM CPN60β1 and 10 μM co-chaperonins, as indicated, was run on a Superdex 200 column with buffer containing 50 μM ADP-AlF3. Collected fractions were resolved by SDS-PAGE and stained with Coomassie. A representative picture from the UV trace of gel filtration is shown in the bottom panel. b Electron micrograph of CPN60β1 with GroES in the presence of ATP-AlF3. The ‘football’ and ‘bullet’ structures are indicated by yellow and red arrows, respectively. c ATPase activity of CPN60β oligomers. The ATP hydrolysis rate of 0.2 μM chaperonin in the presence or absence of 0.4 μM co-chaperonins was measured for 10 min at 25 °C. The data was obtained with three independent experimental replicates and standard deviations are shown. d Functional complementation of GroEL by CPN60β1. The expression of CPN60β and selected co-chaperonin was induced with 1 mM IPTG in GroEL-deficient E. coli strain, MGM100. The strains were grown on medium supplemented with glucose and IPTG at 37 °C for 15 hours

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