Proteome Study of Degradation of Aromatic Hydrocarbons Via Gentisate Pathway
- VernacularTitle:芳香烃龙胆酸降解途径蛋白质组学的研究
- Author:
Yu ZHAO
- Publication Type:Journal Article
- Keywords:
Pseudomonas alcaligenes, Proteome, Gentisate pathway enzymes, 2D-PAGE
- From:
Microbiology
1992;0(04):-
- CountryChina
- Language:Chinese
-
Abstract:
Aromatic hydrocarbons are capital environmental contaminations. Pseudomonas alcaligenes NCIB 9867 (P25X) is capable of degrading aromatic hydrocarbons via the gentisate pathway. Biochemical characterization indicated that it has isofunctional enzymes for the mono- and dioxygenase- catalysed reactions. One set of the enzymes is constitutive and the other is strictly inducible. To date, only the genes for the constitutively-expressed gentisate dioxygenase and the downstream enzymes have been cloned. A mutant strain of P25X, designated SNZ28, which had the constitutive copy of the gentisate 1, 2-dioxygenase gene interrupted by a streptomycin/spectinomycin resistance gene cassette, was found to still express gentisate dioxygenase when induced by gentisate. The proteome profiles of P25X and mutant SNZ28, grown in the presence and absence of the aromatic inducer gentisate, were compared after 2D-PAGE. Fifteen distinctive protein spots which were observed only in induced cells of P25X and mutant SNZ28 but absent in non-induced cells of both were further analyzed by MALDI-TOF and Q-TOF. Of the 15 proteins, 12 showed significant sequence similarity to proteins with assigned function in other microorganisms . The identification of protein P4 which showed positive identification to a gentisate dioxygenase from Ralstonia species indicated the putative role of this protein to encode gentisate 1, 2-dioxygenase in P.alcaligenes.
