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Trigger Factor (TF) is the first chaperone thatinteracts with nascent chains of cytosolic proteins in Escherichia coli.Although its chaperone activity requires association with ribosomes, TF ispresent in vivo in a 2 3 fold molar excess over ribosomes and a fraction of itis not ribosomeassociated after cell lysis. Here we show that TF follows athreestate equilibrium. Size exclusion chromatography, crosslinking andanalytical ultracentrifugation revealed that uncomplexed TF dimerizes with anapparent Kd of 18 M. Dimerization is mediated by the Nterminal ribosome bindingdomain and the Cterminal domain of TF, whereas the central peptidyl prolylisomerase (PPIase) and substrate binding domain does not contribute todimerization. Crosslinking experiments showed that TF is monomeric in itsribosomeassociated state. Quantitative analysis of TF binding to ribosomesrevealed a dissociation constant for the TFribosome complex of approximately1.2 M. From these data we estimate that in vivo most of the ribosomes are incomplex with monomeric TF. Uncomplexed TF, however, is in a monomerdimerequilibrium with approximately two thirds of TF existing in a dimericstate.

Three-State Equilibrium of Escherichia coli Trigger Factor