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Science 4 October 1996:
Vol. 274. no. 5284, pp. 103 - 106
DOI: 10.1126/science.274.5284.103
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Reports

Promotion of Mitochondrial Membrane Complex Assembly by a Proteolytically Inactive Yeast Lon

Martijn Rep, * Jan Maarten van Dijl, * Kitaru Suda, Gottfried Schatz, Leslie A. Grivell, Carolyn K. Suzuki dagger

Afg3p and Rca1p are adenosine triphosphate (ATP)-dependent metalloproteases in yeast mitochondria. Cells lacking both proteins exhibit defects in respiration-dependent growth, degradation of mitochondrially synthesized proteins, and assembly of inner-membrane complexes. Defects in growth and protein assembly, but not in degradation, were suppressed by overproduction of yeast mitochondrial Lon, an ATP-dependent serine protease. Suppression by Lon was enhanced by inactivation of the proteolytic site and was prevented by mutation of the ATP-binding site. It is suggested that the mitochondrial proteases Lon, Afg3p, and Rca1p can also serve a chaperone-like function in the assembly of mitochondrial protein complexes.

M. Rep and L. A. Grivell, Section for Molecular Biology, Department of Molecular Cell Biology, University of Amsterdam, Kruislaan 318, 1098 SM Amsterdam, Netherlands.
J. M. van Dijl, K. Suda, G. Schatz, C. K. Suzuki, Abteilung Biochemie, Biozentrum der Universität Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed.

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