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Vol. 12, Issue 8, 2482-2496, August 2001
*Consiglio Nazionale delle Ricerche, Cellular and Molecular
Pharmacology Center and Department of Medical Pharmacology, University
of Milan, Milan, Italy; and Many mitochondrial outer membrane (MOM) proteins have a
transmembrane domain near the C terminus and an N-terminal cytosolic moiety. It is not clear how these tail-anchored (TA) proteins posttranslationally select their target, but C-terminal charged residues play an important role. To investigate how discrimination between MOM and endoplasmic reticulum (ER) occurs, we used mammalian cytochrome b5, a TA protein existing in two,
MOM or ER localized, versions. Substitution of the seven C-terminal
residues of the ER isoform or of green fluorescent protein reporter
constructs with one or two arginines resulted in MOM-targeted proteins,
whereas a single C-terminal threonine caused promiscuous localization. To investigate whether targeting to MOM occurs from the cytosol or
after transit through the ER, we tagged a MOM-directed construct with a
C-terminal N-glycosylation sequence. Although in vitro this construct was efficiently glycosylated by microsomes, the protein
expressed in vivo localized almost exclusively to MOM, and was nearly
completely unglycosylated. The small fraction of glycosylated protein
was in the ER and was not a precursor to the unglycosylated form. Thus,
targeting occurs directly from the cytosol. Moreover, ER and MOM
compete for the same polypeptide, explaining the dual localization of
some TA proteins.
Faculty of Pharmacy,
University of Catanzaro "Magna Graecia," Catanzaro, Italy
Corresponding author. E-mail address:
Nica{at}csfic.mi.cnr.it.
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