Reversal of the orientation of an integral protein of the mitochondrial outer membrane.
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.
Li
J M
JM
Department of Biochemistry, McGill University, Montreal, Canada.
Shore
G C
GC
D000595:Amino Acid Sequence; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000737:chemistry; D007425:Intracellular Membranes / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D008928:Mitochondria / Q000648:ultrastructure*; D008969:Molecular Sequence Data; D010957:Plasmids; D021382:Protein Sorting Signals / Q000737:chemistry; D051381:Rats; D014162:Transfection; D015003:Yeasts
D005656:Fungal Proteins; D008565:Membrane Proteins; D021382:Protein Sorting Signals