Please use this identifier to cite or link to this item:
Title: A theoretical and experimental proteome map of Pseudomonas aeruginosa PAO1.
Authors: Lecoutere, Elke
Verleyen, Peter
Haenen, Steven
Vandersteegen, Katrien
NOBEN, Jean-Paul 
ROBBEN, Johan 
Schoofs, Liliane
Ceyssens, Pieter-Jan
Volckaert, Guido
Lavigne, Rob
Issue Date: 2012
Source: MICROBIOLOGYOPEN, 1 (2), p. 169-181
Abstract: A total proteome map of the Pseudomonas aeruginosa PAO1 proteome is presented, generated by a combination of two dimensional gel electrophoresis and protein identfication 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 might 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.
Keywords: mass spectrometry (MS); proteomics; two-dimensional gel electrophoresis (2-DE)
Document URI:
ISSN: 2045-8827
e-ISSN: 2045-8827
DOI: 10.1002/mbo3.21
Category: A1
Type: Journal Contribution
Validations: vabb 2014
Appears in Collections:Research publications

Show full item record


checked on Sep 6, 2020


checked on May 22, 2022

Page view(s)

checked on May 27, 2022

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.