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Vol. 273, Issue 3, 1420-1424, January 16, 1998

GTP Hydrolysis Is Essential for Protein Import into the Mitochondrial Matrix

From the Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6085

Protein import into the innermost compartment of mitochondria (the matrix) requires a membrane potential () across the inner membrane, as well as ATP-dependent interactions with chaperones in the matrix and cytosol. The role of nucleoside triphosphates other than ATP during import into the matrix, however, remains to be determined. Import of urea-denatured precursors does not require cytosolic chaperones. We have therefore used a purified and urea-denatured preprotein in our import assays to bypass the requirement of external ATP. Using this modified system, we demonstrate that GTP stimulates protein import into the matrix; the stimulatory effect is directly mediated by GTP hydrolysis and does not result from conversion of GTP to ATP. Both external GTP and matrix ATP are necessary; neither one can substitute for the other if efficient import is to be achieved. These results suggest a "push-pull" mechanism of import, which may be common to other post-translational translocation pathways.

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