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Identification by mass spectrometry of two‐dimensional gel electrophoresis‐separated proteins extracted from lager brewing yeast
Author(s) -
Jouber Richard,
Strub JeanMarc,
Zugmeyer Sandra,
Kobi Dominique,
Carte Nathalie,
Van Dorsselaer Alain,
Boucherie Hélian,
JaquetGutfreund Laurence
Publication year - 2001
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(200108)22:14<2969::aid-elps2969>3.0.co;2-4
Subject(s) - proteome , saccharomyces cerevisiae , yeast , mass spectrometry , brewing , gel electrophoresis , proteomics , tandem mass spectrometry , computational biology , protein mass spectrometry , chemistry , genome , identification (biology) , biochemistry , biology , chromatography , gene , fermentation , botany
As two‐dimensional (2‐D) electrophoresis allows the separation of several hundred proteins in a single gel, this technique has become an important tool for proteome studies and for investigating the cellular physiology. In order to take advantage of information provided by the comparison of proteome pictures, the mass spectrometry technique is the way chosen for a rapid and an accurate identification of proteins of interest. Unfortunately, in the case of industrial yeasts, due to the high level of complexity of their genome, the whole DNA sequence is not yet available and all encoded protein sequences are still unknown. Nevertheless, this study presents here 30 lager brewing yeast proteins newly identified with matrix assisted laser desorption/ionization‐time of flight (MALDI‐TOF), tandem mass spectrometry (MS/MS) and database searching against the protein sequences of Saccharomyces cerevisiae . The identified proteins of the industrial strain correspond to proteins which do not comigrate with known proteins of S. cerevisiae separated on 2‐D gels. This study presents an application of the MS technique for the identification of industrial yeast proteins which are only homologous to the corresponding S. cerevisiae proteins.