A theoretical and experimental proteome map of Pseudomonas aeruginosa PAO1

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Abstract

A total proteome map of the Pseudomonas aeruginosa PAO1 proteome is presented, generated by a combination of two-dimensional gel electrophoresis and protein identification by mass spectrometry. In total, 1128 spots were visualized, and 181 protein spots were characterized, corresponding to 159 different protein entries. In particular, protein chaperones and enzymes important in energy conversion and amino acid biosynthesis were identified. Spot analysis always resulted in the identification of a single protein, suggesting sufficient spot resolution, although the same protein may be detected in two or more neighboring spots, possibly indicating posttranslational modifications. Comparison to the theoretical proteome revealed an underrepresentation of membrane proteins, though the identified proteins cover all predicted subcellular localizations and all functional classes. These data provide a basis for subsequent comparative studies of the biology and metabolism of P. aeruginosa, aimed at unraveling global regulatory networks. © 2012 The Authors.

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Lecoutere, E., Verleyen, P., Haenen, S., Vandersteegen, K., Noben, J. P., Robben, J., … Lavigne, R. (2012). A theoretical and experimental proteome map of Pseudomonas aeruginosa PAO1. MicrobiologyOpen, 1(2), 169–181. https://doi.org/10.1002/mbo3.21

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