Issue 3, 2011
From the journal:

Molecular BioSystems

Long signal peptides of RGMa and DCBLD2 are dissectible into subdomains according to the NtraC model†

Eduard Resch,‡*a   Jan A. Hiss,‡b   Alexander Schreiner,§a   Gisbert Schneiderb  and  Anna Starzinski-Powitza  

* Corresponding authors

a Institute for Cell Biology and Neuroscience, Molecular Cell Biology and Human Genetics, Johann Wolfgang Goethe University of Frankfurt, Siesmayerstrasse 70, Germany
E-mail: e.resch@bio.uni-frankfurt.de
Fax: +49 6979824732
Tel: +49 6979824809

b Institute of Pharmaceutical Sciences, Eidgenössische Technische Hochschule (ETH), Wolfgang-Pauli-Str. 10, CH-8093 Zürich, Switzerland

Abstract

Targeting of proteins to the endoplasmic reticulum (ER) usually requires N-terminal signal peptides (SP) of approximately 22 amino acids in length. However, a substantial number of proteins contain exceptionally long SPs of 40 amino acids and more, an example being protein shrew-1/AJAP1. Using shrew-1's SP as example, the NtraC model has been developed by dissecting long SPs into two functionally distinct subdomains (“N” and “C”) separated by a β-turn rich transition area (“tra”). Further proteins have been identified by computational analysis complying with the NtraC model. Here we used the SPs of two of these proteins, DCBLD2 and RGMa (including three isoforms), to show that the NtraC model applies to a growing group of SPs. We demonstrate that the full-length SPs of RGMa and DCBLD2 are functional and furthermore that the C-domains are sufficient and essential for ER targeting, whereas the N-domains are dispensable. Thus, the N-domains are available for additional functions.

Graphical abstract: Long signal peptides of RGMa and DCBLD2 are dissectible into subdomains according to the NtraC model

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Article information

DOI
https://doi.org/10.1039/C0MB00254B
Article type
Paper
Submitted
29 Oct 2010
Accepted
30 Nov 2010
First published
24 Dec 2010

Mol. BioSyst., 2011,7, 942-951

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Long signal peptides of RGMa and DCBLD2 are dissectible into subdomains according to the NtraC model

E. Resch, J. A. Hiss, A. Schreiner, G. Schneider and A. Starzinski-Powitz, Mol. BioSyst., 2011, 7, 942 DOI: 10.1039/C0MB00254B

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