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Originally published as Genetics Published Articles Ahead of Print on February 16, 2005.
Genetics, Vol. 170, 139-148, May 2005, Copyright © 2005
doi:10.1534/genetics.104.039933
Drosophila Signal Peptide Peptidase Is an Essential Protease for Larval Development
David J. Casso*,
Soichi Tanda
,
Brian Biehs*,
Bruno Martoglio
and
Thomas B. Kornberg*,1
* Department of Biochemistry and Biophysics, University of California, San Francisco, California 94143
Department of Biological Sciences, Ohio University, Athens, Ohio 45701
Institute of Biochemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, 8093 Zürich, Switzerland
1 Corresponding author: Department of Biochemistry and Biophysics, 1550 4th St., University of California, San Francisco, CA 94143.
E-mail: tkornberg{at}biochem.ucsf.edu
We identified the Drosophila melanogaster Signal peptide peptidase gene (Spp) that encodes a multipass transmembrane aspartyl protease. Drosophila SPP is homologous to the human signal peptide peptidase (SPP) and is distantly related to the presenilins. We show that, like human SPP, Drosophila SPP can proteolyze a model signal peptide and is sensitive to an SPP protease inhibitor and that it localizes to the endoplasmic reticulum. Expression of Drosophila SPP was first apparent at germ band extension, and in late embryos it was robust in the salivary glands, proventriculus, and tracheae. Flies bearing mutations in conserved residues or carrying deficiencies for the Spp gene had defective tracheae and died as larvae.
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