Strong precursor-pore interactions constrain models for mitochondrial protein import

Mitochondrial precursor proteins are imported from the cytosol into the matrix compartment through a proteinaceous translocation pore. Import is driven by mitochondrial Hsp70 (mHsp70), a matrix-localized ATPase. There are currently two postulated mechanisms for this function of mHsp70: 1) The "Brownian ratchet" model proposes that the precursor chain diffuses within the pore, and that binding of mHsp70 to the lumenal portion of the chain biases this diffusion. 2) The "power stroke" model proposes that mHsp70 undergoes a conformational change that actively pulls the precursor chain through the pore. Here we formulate these two models quantitatively, and compare their performance in light of recent experimental evidence that precursor chains interact strongly with the walls of the translocation pore. Under these conditions the simulated Brownian ratchet is inefficient, whereas the power stroke mechanism seems to be a plausible description of the import process.