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Science 26 June 1992:
Vol. 256. no. 5065, pp. 1815 - 1817
DOI: 10.1126/science.1615327
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Articles

Science, Vol 256, Issue 5065, 1815-1817
Copyright © 1992 by American Association for the Advancement of Science

articles

Reversal of the orientation of an integral protein of the mitochondrial outer membrane

JM Li and GC Shore

Department of Biochemistry, McGill University, Montreal, Canada.

The NH2-terminus of the signal-anchor sequence of an integral, bitopic protein of the outer mitochondrial membrane was extended both in amino acid length (from 11 to 38 amino acids) and net charge (from +4 to +8)--changes that confer on the NH2-terminus characteristics of a strong matrix-targeting signal. The protein was inserted into the outer membrane but in an inverted orientation (Ncyto-Cin). These findings suggest that, in common with other membrane systems, the orientation of a protein in the outer mitochondrial membrane can be determined by a signal that causes retention of the NH2-terminus on the cytosolic side of the membrane.


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