Adaptation to β-myrcene catabolism in Pseudomonas sp. M1: An expression proteomics analysis

Authors

  • Pedro M. Santos,

    Corresponding author
    1. IBB-Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Lisboa, Portugal
    Current affiliation:
    1. CBMA-Centre of Molecular and Environmental Biology, Department of Biology, University of Minho, Campus de Gualtar, 4715-057 Braga, Portugal.
    • IBB-Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal Fax: +351-218419199
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  • Isabel Sá-Correia

    1. IBB-Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Lisboa, Portugal
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Abstract

β-Myrcene, a monoterpene widely used as a fragrance and flavoring additive, also possesses analgesic, anti-mutagenic, and tyrosinase inhibitory properties. In order to get insights into the molecular mechanisms underlying the ability of Pseudomonas sp. M1 to catabolize β-myrcene, an expression proteomics approach was used in this study. Results indicate that the catabolic enzyme machinery for β-myrcene utilization (MyrB, MyrC, and MyrD and other uncharacterized proteins) is strongly induced when β-myrcene is present in the growth medium. Since an M1 mutant, lacking a functional 2-methylisocitrate dehydratase, is not able to grow in mineral medium with β-myrcene or propionic acid as the sole C-source, and also based on the expression proteomic analysis carried out in this study, it is suggested that the β-myrcene catabolic intermediate propionyl-CoA is channeled into the central metabolism via the 2-methylcitrate cycle. Results also suggest that the major alteration occurring in the central carbon metabolism of cells growing in β-myrcene-containing media is related with the redistribution of the metabolic fluxes leading to increased oxaloacetate production. Other up-regulated proteins are believed to prevent protein misfolding and aggregation or to play important structural roles, contributing to the adaptive alteration of cell wall and membrane organization and integrity, which are essential features to allow the bacterium to cope with the highly lipophilic β-myrcene as C-source.

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