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Proteome analysis of Schizosaccharomyces pombe by two‐dimensional gel electrophoresis and mass spectrometry
Author(s) -
Hwang KyungHoon,
Carapito Christine,
Böhmer Susanne,
Leize Emmanuelle,
Van Dorsselaer Alain,
Bernhardt Rita
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500863
Subject(s) - schizosaccharomyces pombe , proteome , yeast , proteomics , biology , schizosaccharomyces , mass spectrometry , computational biology , eukaryote , biochemistry , genetics , saccharomyces cerevisiae , gene , chemistry , genome , chromatography
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 p I 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).