Article abstract


Nature Biotechnology 25, 576 - 583 (2007)
Published online: 22 April 2007 | doi:10.1038/nbt1300

A high-quality catalog of the Drosophila melanogaster proteome

Erich Brunner1,10, Christian H Ahrens1,2,10, Sonali Mohanty1,3,10, Hansruedi Baetschmann2, Sandra Loevenich1,3, Frank Potthast2, Eric W Deutsch4, Christian Panse2, Ulrik de Lichtenberg5,6, Oliver Rinner3, Hookeun Lee3, Patrick G A Pedrioli3, Johan Malmstrom3, Katja Koehler3, Sabine Schrimpf1,7, Jeroen Krijgsveld8, Floyd Kregenow4, Albert J R Heck8, Ernst Hafen3, Ralph Schlapbach2 & Ruedi Aebersold3,9


Understanding how proteins and their complex interaction networks convert the genomic information into a dynamic living organism is a fundamental challenge in biological sciences. As an important step towards understanding the systems biology of a complex eukaryote, we cataloged 63% of the predicted Drosophila melanogaster proteome by detecting 9,124 proteins from 498,000 redundant and 72,281 distinct peptide identifications. This unprecedented high proteome coverage for a complex eukaryote was achieved by combining sample diversity, multidimensional biochemical fractionation and analysis-driven experimentation feedback loops, whereby data collection is guided by statistical analysis of prior data. We show that high-quality proteomics data provide crucial information to amend genome annotation and to confirm many predicted gene models. We also present experimentally identified proteotypic peptides matching approx50% of D. melanogaster gene models. This library of proteotypic peptides should enable fast, targeted and quantitative proteomic studies to elucidate the systems biology of this model organism.

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  1. Center for Model Organism Proteomes, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
  2. Functional Genomics Center, ETH and University of Zurich, Winterthurerstrasse 190, Y55L70, 8057 Zurich, Switzerland.
  3. Institute for Molecular Systems Biology, Swiss Federal Institute of Technology, ETH Honggerberg, Wolfgang-Pauli-Str. 16, HPT, CH-8093 Zurich, Switzerland.
  4. Institute for Systems Biology, 1441 N. 34th Street, Seattle, Washington 98103, USA.
  5. Center for Biological Sequence Analysis, BioCentrum-DTU, Technical, University of Denmark, Kemitorvet, Building 208, DK-2800 Lyngby, Denmark.
  6. LEO Pharma, Industriparken 55, DK2750 Ballerup, Denmark.
  7. Institute for Molecular Biology, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
  8. Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, the Netherlands.
  9. Faculty of Science, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
  10. These authors contributed equally to this work.

Correspondence to: Ruedi Aebersold3,9 e-mail: aebersold@imsb.biol.ethz.ch

Correspondence to: Erich Brunner1,10 e-mail: erich.brunner@molbio.uzh.ch

Correspondence to: Christian H Ahrens1,2,10 e-mail: christian.ahrens@fgcz.ethz.ch


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