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Papers In Press, published online ahead of print November 22, 2002
Section of Cellular and Molecular Pharmacology, Consiglio Nazionale delle Ricerche Institute for Neuroscience, Milano 20129
Corresponding Author: Nica{at}csfic.mi.cnr.it
C-tail anchored proteins are defined by an N-terminal cytosolic domain followed by a transmembrane anchor close to the C-terminus. Their extreme C-terminal polar residues are translocated across membranes by poorly understood posttranslational mechanism(s). Here we used the yeast system to study translocation of the C-terminus of a tagged form of mammalian cytochrome b(5), carrying an N-glycosylation site in its C-terminal domain (b(5)-Nglyc). Utilization of this site was adopted as a rigorous criterion for translocation across the ER membrane of yeast wild-type and mutant cells. The C-terminus of b(5)-Nglyc was rapidly glycosylated in mutants where Sec61p was defective and incapable of translocating carboxypeptidase Y, a well known substrate for post-translational translocation. Likewise, inactivation of several other components of the translocon machinery had no effect on b(5)-Nglyc translocation. The kinetics of translocation were faster for b(5)-Nglyc than for a signal peptide-containing reporter. Depletion of the cellular ATP pool to a level which retarded Sec61p-dependent post-translational translocation still allowed translocation of b(5)-Nglyc. Similarly, only low ATP concentrations (below 1 microM), in addition to cytosolic protein(s), were required for in vitro translocation of b(5)-Nglyc into mammalian microsomes. Thus, translocation of tail-anchored b(5)-Nglyc proceeds by a mechanism different from that of signal peptide-driven post-translational translocation.
J. Biol. Chem, 10.1074/jbc.M210253200
Submitted on October 7, 2002
Revised on November 11, 2002
Accepted on November 22, 2002
Translocation of the C-terminus of a tail-anchored protein across the endoplasmic reticulum membrance in yeast mutants defective in signal peptide-driven translocation
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