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doi:10.1534/genetics.104.039933
A more recent version of this article appeared on May 1, 2005.
REGULAR RESEARCH PAPERS |
Drosophila Signal Peptide Peptidase is an essential protease for larval development
David J Casso 1, Soichi Tanda 2, Brian Biehs 1, Bruno Martoglio 3 and Thomas B Kornberg 1*
1 UCSF Cancer Center
2 Ohio University
3 Swiss Federal Institute of Technology
* To whom correspondence should be addressed. E-mail: tkornberg{at}biochem.ucsf.edu.
Submitted on December 15, 2004
Revised on January 12, 2005
Accepted on 12 January 2005
We identified the Drosophila melanogaster signal peptide peptidase gene (spp) which encodes a multi-pass 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.
Key Words: intramembrane protease, larval lethal, signal peptide protease, tracheal development
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