Proteome analysis of cellular response of Pseudomonas putida KT2440 to tetracycline stress

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Proteome analysis of cellular response of Pseudomonas putida KT2440 to tetracycline stress
S H Yun; Y H Kim; E J Joo; J S Choi; Jung Hoon Sohn; S I Kim
Bibliographic Citation
Current Microbiology, vol. 53, no. 2, pp. 95-101
Publication Year
Tetracycline-induced proteome of Pseudomonas putida KT2440 was analyzed by 2-D gel electrophoresis and matrix-assisted laser desorption ionization-time of flight/mass spectrum (NALDI-TOF/MS) in order to understand cellular response to tetracycline. of the proteins upregulated in a culture medium containing subinhibitory concentration of tetracycline (50 μg/mL), we identified 38 proteins from cytosol and precipitated fractions by peptide mass fingerprinting and mass spectrum/mass spectrum analysis. Various amino acids ABC transporters, a ribose ABC transporter, and a sulfate ABC transporter were found to be upregulated. Protein synthesis-related proteins, stress proteins, energy metabolic enzymes, and unknown proteins were also strongly induced. of the identified upregulated proteins, several proteins (isocitrate lyase, branched-chain amino acid ABC transporter, superoxide dismutase, etc.) were also upregulated under phenol-induced stress condition. These results demonstrate that tetracycline at a high concentration induced comprehensive stress in P. putida KT2440 and the global induction of proteins related to bacteria survival. Proteome analysis was found to be a useful tool for the elucidation of antibiotic-induced proteins in the present study.
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Synthetic Biology and Bioengineering Research Institute > Synthetic Biology Research Center > 1. Journal Articles
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