Volume 6, Issue 14 p. 4115-4129
Microbiology

Proteome analysis of Schizosaccharomyces pombe by two-dimensional gel electrophoresis and mass spectrometry

Kyung-Hoon Hwang

Kyung-Hoon Hwang

Universität des Saarlandes, FR 8.3 Biochemie, Saarbrücken, Germany

These authors contributed equally to this work.

Search for more papers by this author
Christine Carapito

Christine Carapito

Laboratoire de Spectrométrie de Masse Bio-Organique, UMR 7512 CNRS/ULP, ECPM, Strasbourg, France

These authors contributed equally to this work.

Search for more papers by this author
Susanne Böhmer

Susanne Böhmer

Universität des Saarlandes, FR 8.3 Biochemie, Saarbrücken, Germany

Search for more papers by this author
Emmanuelle Leize

Emmanuelle Leize

Laboratoire de Spectrométrie de Masse Bio-Organique, UMR 7512 CNRS/ULP, ECPM, Strasbourg, France

Search for more papers by this author
Alain Van Dorsselaer

Alain Van Dorsselaer

Laboratoire de Spectrométrie de Masse Bio-Organique, UMR 7512 CNRS/ULP, ECPM, Strasbourg, France

Search for more papers by this author
Rita Bernhardt Dr.

Corresponding Author

Rita Bernhardt Dr.

Universität des Saarlandes, FR 8.3 Biochemie, Saarbrücken, Germany

Universität des Saarlandes, FR 8.3 Biochemie, P.O. Box 151150, D-66041 Saarbrücken, Germany Fax: +49-681-302-4739===Search for more papers by this author
First published: 18 July 2006
Citations: 17

Abstract

The fission yeast Schizosaccharomyces pombe (S. pombe) is a unicellular eukaryote and contains many genes and regulatory mechanisms that are close to those of mammals. In this study, we performed a global proteomic analysis of the fission yeast S. pombe wild type h−S L 972 proteome. More than 1500 protein spots were visualized on silver stained 2-D gels in the 3–10 pI range with a high resolution and high reproducibility. Protein identification was carried out by MALDI-TOF-MS and/or nanoLC-MS/MS. Advantage of the complementarity of these two MS approaches was used to enhance the identification quality. So far, 364 proteins (representing 157 different proteins) have been identified. We report here the identification of 117 new proteins on our 2-D reference map of this yeast compared to the first reference map. Of these identified proteins, 40.1% were involved in metabolism. The present work provides a very useful tool for all studies relying on S. pombe as a model organism and is a considerable complement to the first reference map of S. pombe published recently by Sun and coworkers (Sun, N., Jang, J., Lee, S., Kim, S. et al.., Proteomics 2005, 5, 1574–1579).