Analysis of protein sequences and protein complexes by matrix-assisted laser desorption/ionization mass spectrometry

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Eur. J. Mass Spectrom. 7, 101 - 109 (2001)

Analysis of protein sequences and protein complexes by matrix-assisted laser desorption/ionization mass spectrometry

Maya Belghazi and Katell Bathany
Institut Européen de Chimie Biologie, 33607 Pessac, France
Codjo Hountondji
Laboratoire de Biochimie, UMR CNRS 7654, Ecole Polytechnique, 91128 Palaiseau, France
Xavier Grandier-Vazeille and St‚phen Manon
Institut de Biologie et Génétique Cellulaire du CNRS, 33077 Bordeaux, France
Jean-Marie Schmitter^*
Laboratoire de Physico-Toxico-Chimie, UMR CNRS 5472 Université Bordeaux I, 33405 Talence, France

ABSTRACT:

In the context of proteome analysis, matrix-assisted laser desorption/ionization (MALDI) mass spectrometry can fulfil the two tasks of primary structure verification and protein identification. As an illustration of the first of these tasks, the sequence of E. coli isoleucyl-tRNA synthetase, a protein with 15 reported sequence conflicts, has been established by means of MALDI mass mapping. The identification of mitochondrial proteins participating in a yeast supramolecular complex exhibiting NADH dehydrogenase activity highlights the performance of MALDI mass spectrometry for the second task. The spectral suppression phenomenon occurring for complex peptide mixtures analyzed by MALDI is discussed, as well as the role of post-source decay (PSD) analysis for confident protein identification.

Keywords: matrix-assisted laser desorption/ionization, spectral suppression, post-source decay, proteome analysis, protein sequence verification, supramolecular protein complex, yeast NADH dehydrogenases, aminoacyl-tRNA synthetases

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