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Identification by mass spectrometry of two-dimensional gel electrophoresis-separated proteins extracted from lager brewing yeast.
Electrophoresis. 2001 Aug; 22(14):2969-82.E

Abstract

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.

Authors+Show Affiliations

Joubert R
TEPRAL Research Center, Les Brasseries Kronenbourg, Strasbourg, France.
Strub JM
No affiliation info available
Zugmeyer S
No affiliation info available
Kobi D
No affiliation info available
Carte N
No affiliation info available
Van Dorsselaer A
No affiliation info available
Boucherie H
No affiliation info available
Jaquet-Guffreund L
No affiliation info available

MeSH

AcetyltransferasesAmino Acid SequenceComputer SimulationElectrophoresis, Gel, Two-DimensionalIndustrial MicrobiologyMolecular Sequence DataPeptide MappingProtein IsoformsSaccharomycesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSpecies SpecificitySpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Pub Type(s)

Comparative Study
Journal Article

Language

eng

PubMed ID

11565791

Citation

Joubert, R, et al. "Identification By Mass Spectrometry of Two-dimensional Gel Electrophoresis-separated Proteins Extracted From Lager Brewing Yeast." Electrophoresis, vol. 22, no. 14, 2001, pp. 2969-82.
Joubert R, Strub JM, Zugmeyer S, et al. Identification by mass spectrometry of two-dimensional gel electrophoresis-separated proteins extracted from lager brewing yeast. Electrophoresis. 2001;22(14):2969-82.
Joubert, R., Strub, J. M., Zugmeyer, S., Kobi, D., Carte, N., Van Dorsselaer, A., Boucherie, H., & Jaquet-Guffreund, L. (2001). Identification by mass spectrometry of two-dimensional gel electrophoresis-separated proteins extracted from lager brewing yeast. Electrophoresis, 22(14), 2969-82.
Joubert R, et al. Identification By Mass Spectrometry of Two-dimensional Gel Electrophoresis-separated Proteins Extracted From Lager Brewing Yeast. Electrophoresis. 2001;22(14):2969-82. PubMed PMID: 11565791.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Identification by mass spectrometry of two-dimensional gel electrophoresis-separated proteins extracted from lager brewing yeast. AU - Joubert,R, AU - Strub,J M, AU - Zugmeyer,S, AU - Kobi,D, AU - Carte,N, AU - Van Dorsselaer,A, AU - Boucherie,H, AU - Jaquet-Guffreund,L, PY - 2001/9/22/pubmed PY - 2002/4/9/medline PY - 2001/9/22/entrez SP - 2969 EP - 82 JF - Electrophoresis JO - Electrophoresis VL - 22 IS - 14 N2 - 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. SN - 0173-0835 UR - https://www.unboundmedicine.com/medline/citation/11565791/Identification_by_mass_spectrometry_of_two_dimensional_gel_electrophoresis_separated_proteins_extracted_from_lager_brewing_yeast_ L2 - https://doi.org/10.1002/1522-2683(200108)22:14<2969::AID-ELPS2969>3.0.CO;2-4 DB - PRIME DP - Unbound Medicine ER -