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Focusing on substitutions that occurred in such regions, we identified historical changes that drastically reduced Rubisco’s activity but whose negative effect is buffered by the presence of the SSU.

Inspired by NMR-guided directed evolution, we used hydrogen-deuterium exchange experiments to identify structural features of Rubisco that change their deuterium uptake behavior (which, in very condensed form, can be indicative of altered protein dynamics) upon inhibitor binding.

We found that historical substitutions at the dimer-dimer interface made octamer formation SSU-dependent. The SSU bridges adjacent dimers, which stabilizes the dimer-dimer interface. This allows evolution to explore a less stable interface. But why is octamer formation important?

Form I Rubiscos assemble into an octamer of large subunits (purple) that is capped by small subunits (SSU) at the bottom and top of the complex (beige). This stoichiometry evolved from a simple octamer of large subunits and the SSU subsequently became essential for the complex.