Insights from comparative proteomic analysis into degradation of phenanthrene and salt tolerance by the halophilic Martelella strain AD-3.

ABSTRACT

A halophilic PAHs-degrading strain, Martelella AD-3, was previously isolated from highly saline petroleum-contaminated soil. In this study, label-free proteomics were performed to identify differentially expressed proteins (DEPs) under Group P (phenanthrene +5% salinity) and Group G (glycerol +1% salinity), which would help to reveal the mechanism of phenanthrene degradation and salt tolerance. A total of 307 up-regulated DEPs were found in Group P, including 17 phenanthrene degradation proteins. Among these phenanthrene-degrading proteins, the ferredoxin of aromatic ring-hydroxylating dioxygenase (RHD) was up-regulated by 110-fold and gentisate 1,2-dioxygenases (GDOs) were only expressed in Group P. Besides, we also found nine high salt stress response proteins, including ectoine synthase and transport protein of compatible (osmoprotectant) solutes, were differentially up-regulated. These results indicate that strain AD-3 mainly relied on RHD and dihydrodiol dehydrogenase to degrade phenanthrene, and accumulated compatible solutes for resistance to salt stress. This study provides strong theoretical guidance for understanding the degradation of phenanthrene by strain AD-3 in high salt environments.