Skip to main content
. Author manuscript; available in PMC: 2012 Dec 10.
Published in final edited form as: Adv Exp Med Biol. 2012;751:139–156. doi: 10.1007/978-1-4614-3567-9_7

Fig. 7.3. Evolution of co-complex interactions in the group II chaperonins.

Fig. 7.3

Computational studies have shown that protein complexes usually evolve by duplication and divergence of their subunits. The group II chaperonin complexes provide a good illustration of this general trend. The archeal group II chaperonin complexes (termed thermosomes) usually contain 1–3 homologous chaperonins and it represented here by the thermosome of Thermococcus strain KS-1 (PDB:1Q2V). The eukaryotic complexes (called TriC or CCT) are composed of eight chaperonin paralogs, represented here by the S. cerevisiae CCT complex (PDB:3P9E). All of the subunits are structurally similar, exemplified here by the S. cerevisiae CCT1 subunit structure