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Originally published In Press as doi:10.1074/jbc.M210253200 on November 22, 2002

J. Biol. Chem., Vol. 278, Issue 5, 3489-3496, January 31, 2003
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Translocation of the C Terminus of a Tail-anchored Protein across the Endoplasmic Reticulum Membrane in Yeast Mutants Defective in Signal Peptide-driven Translocation*

Monica YabalDagger §, Silvia Brambillasca, Paolo Soffientini, Emanuela Pedrazzini||, Nica Borgese**Dagger Dagger , and Marja MakarowDagger §§§

From the Dagger  Program of Cellular Biotechnology, Institute of Biotechnology, University of Helsinki, Viikinkaari 9, 00710 Helsinki, Finland,  Consiglio Nazionale delle Ricerche Institute of Neuroscience, Cellular and Molecular Pharmacology Section, Via Vanvitelli 32-20129 Milano, Italy, and the ** Faculty of Pharmacy, University of Catanzaro "Magna Graecia," 8021 Roccelletta di Borgia (Catanzaro), Italy

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 post-translational mechanism(s). Here we have used the yeast system to study translocation of the C terminus of a tagged form of mammalian cytochrome b5, carrying an N-glycosylation site in its C-terminal domain (b5-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 b5-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 b5-Nglyc translocation. The kinetics of translocation were faster for b5-Nglyc than for a signal peptide-containing reporter. Depletion of the cellular ATP pool to a level that retarded Sec61p-dependent post-translational translocation still allowed translocation of b5-Nglyc. Similarly, only low ATP concentrations (below 1 µM), in addition to cytosolic protein(s), were required for in vitro translocation of b5-Nglyc into mammalian microsomes. Thus, translocation of tail-anchored b5-Nglyc proceeds by a mechanism different from that of signal peptide-driven post-translational translocation.

* This work was supported in part by Associazione Italiana Ricerca sul Cancro (AIRC), Telethon (Grant E734), and the Ministero per la Istruzione, Università e Ricerca (M.I.U.R.- COFIN 2001).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by the University of Helsinki and the Academy of Finland (Grant 53607).

|| Present address: Consiglio Nazionale delle Ricerche Istituto di Biologia e Biotecnologia Agraria, Via Bassini 15-20133 Milano, Italy.

Dagger Dagger To whom correspondence should be addressed. Tel.: 39-02-50316971; Fax: 39-02-7490574; E-mail: nica@csfic.mi.cnr.it.

§§ A Biocentrum Helsinki fellow.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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