Proteomic study of linuron and 3,4-dichloroaniline degradation by Variovorax sp WDL1: evidence for the involvement of an aniline dioxygenase-related multicomponent protein
(2010) Research in Microbiology — Vol. 161, n° 3, p. 208-218 (2010)
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- A proteomic approach was used to explore the metabolism of the phenylurea herbicide linuron and 3.4-dichloroamline (3.4-DCA) in Variovorax sp. WDL1. This bacterium grows on linuron as sole source of carbon, nitrogen and energy, while it transiently accumulates 3,4-DCA as a metabolite Differential protein expression analysis of Vanovorax sp WDLI grown in a heterotrophic medium in the presence and absence of Imuron or 3.4-DCA was conducted using 2-D PAGE Selected up- and downregulatcd proteins were identified with nanoLC-ESI-MS/MS. In the 3,4-DCA-supplemented culture, upregulation of several proteins showing high amino acid sequence similarity to different components of the multicomponent aniline dioxygenase in aniline-degrading Proreobactena was observed. For one of the components, multiple variant proteins were detected, suggesting that strain WDL1 harbors several copies of the aniline dioxygenase (AD) gene cluster which are simultaneously expressed in the presence of 3.4-DCA A number of unidentifiable proteins, which were upreeulated in the hnuron- and/or 3/I-DCA-supplemented cultures, might represent up to now uncharacterized proteins with a role in hnuron and/or 3,4-DCA degradation in strain WDLI In addition, several stress-related proteins were differentially expressed (C) 2010 Elsevier Masson SAS All rights reserved
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Breugelmans, P., Leroy, B., Bers, K., Dejonghe, W., Wattiez, R., De Mot, R., & Springael, D. (2010). Proteomic study of linuron and 3,4-dichloroaniline degradation by Variovorax sp WDL1: evidence for the involvement of an aniline dioxygenase-related multicomponent protein. Research in Microbiology, 161(3), 208-218. https://doi.org/10.1016/j.resmic.2010.01.010 (Original work published 2010)