Well, one of the basic ways that chaperonins work is to block other molecules from interacting with the folding protein. Some proteins have hydrophobic residues that might interact with similar hydrophobic residues on other proteins before the protein finishes folding. This causes aggregation of improperly folded proteins.
Did the 'first cell' have chaperonins? Possibly. In pre-biotic conditions there was almost certainly a complex evolutionary process occurring which acted on RNA and/or maybe other molecules. The existence of a full cell wasn't necessarily required for complex molecular interactions.
I am not familiar with chaperonins in general, but I'll look into it.
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