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Originally published In Press as doi:10.1074/jbc.M000456200 on March 9, 2000
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J Biol Chem, Vol. 275, Issue 20, 14916-14922, May 19, 2000

The Topogenic Contribution of Uncharged Amino Acids on Signal Sequence Orientation in the Endoplasmic Reticulum*

Karin Rösch, Dieter Naeher, Vivienne Laird, Veit Goder, and Martin SpiessDagger

From Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland

Signal sequences for insertion of proteins into the endoplasmic reticulum induce translocation of either the C- or the N-terminal sequence across the membrane. The end that is translocated is primarily determined by the flanking charges and the hydrophobic domain of the signal. To characterize the hydrophobic contribution to topogenesis, we have challenged the translocation machinery in vivo in transfected COS cells with model proteins differing exclusively in the apolar segment of the signal. Homo-oligomers of hydrophobic amino acids as different in size and shape as Val19, Trp19, and Tyr22 generated functional signal sequences with similar topologies in the membrane. The longer a homo-oligomeric sequence of a given residue, the more N-terminal translocation was obtained. To determine the topogenic contribution of all uncharged amino acids in the context of a hydrophobic signal sequence, two residues in a generic oligoleucine signal were exchanged for all uncharged amino acids. The resulting scale resembles a hydrophobicity scale with the more hydrophobic residues promoting N-terminal translocation. In addition, the helix breakers glycine and proline showed a position-dependent effect, which raises the possibility of a conformational contribution to topogenesis.

* This work was supported by Swiss National Science Foundation Grant 31-43483.95 and by a Wellcome Trust Prize Travelling Fellowship (to V. L.).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.

Dagger To whom correspondence should be addressed: Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. Tel.: 41-61-2672164; Fax: 41-61-2672149; E-mail: spiess@ubaclu.unibas.ch.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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