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The Force Exerted by the Membrane Potential during Protein Import into the Mitochondrial Matrix

Karim Shariff ^*, Sandip Ghosal  and Andreas Matouschek 

^* National Aeronautics and Space Administration, Ames Research Center, Moffett Field, California; and Department of Mechanical Engineering, Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois

Correspondence: Address reprint requests to Karim Shariff, NASA Ames Research Center, Physics Simulation and Modeling Office, MS 19-44, Moffett Field, CA 94035. Tel.: 650-604-5361; E-mail: shariff{at}nas.nasa.gov.

The force exerted on a targeting sequence by the electrical potential across the inner mitochondrial membrane is calculated on the basis of continuum electrostatics. The force is found to vary from 3.0 pN to 2.2 pN (per unit elementary charge) as the radius of the inner membrane pore (assumed aqueous) is varied from 6.5 to 12 Å, its measured range. In the present model, the decrease in force with increasing pore width arises from the shielding effect of water. Since the pore is not very much wider than the distance between water molecules, the full shielding effect of water may not be present; the extreme case of a purely membranous pore without water gives a force of 3.2 pN per unit charge, which should represent an upper limit. When applied to mitochondrial import experiments on the protein barnase, these results imply that forces between 11 ± 2 pN and 13.5 ± 2.5 pN catalyze the unfolding of barnase in those experiments. A comparison of these results with unfolding forces measured using atomic force microscopy is made.