Arsenic Methylation and Volatilization by Arsenite S -Adenosylmethionine Methyltransferase in Pseudomonas alcaligenes NBRC14159

• DOI: 10.1128/aem.03804-14
• Publication Date: 2015-02-14T02:46:51Z
• Authors: Jun Zhang; Tingting Cao; Zhu Tang; Qirong Shen; Barry P. Rosen; Fang-Jie Zhao
• Keywords: 0301 basic medicine; 03 medical and health sciences; Bacterial Proteins; Arsenites; Molecular Sequence Data; Amino Acid Sequence; Methyltransferases; Sequence Alignment; Biotransformation; Pseudomonas alcaligenes

ABSTRACT

Inorganic arsenic (As) is highly toxic and ubiquitous in the environment. Inorganic As can be transformed by microbial methylation, which constitutes an important part of the As biogeochemical cycle. In this study, we investigated As biotransformation by Pseudomonas alcaligenes NBRC14159. P. alcaligenes was able to methylate arsenite [As(III)] rapidly to dimethylarsenate and small amounts of trimethylarsenic oxide. An arsenite S -adenosylmethionine methyltransferase, PaArsM, was identified and functionally characterized. PaArsM shares low similarities with other reported ArsM enzymes (<55%). When P. alcaligenes arsM gene ( PaarsM ) was disrupted, the mutant lost As methylation ability and became more sensitive to As(III). PaarsM was expressed in the absence of As(III) and the expression was further enhanced by As(III) exposure. Heterologous expression of PaarsM in an As-hypersensitive strain of Escherichia coli conferred As(III) resistance. Purified PaArsM protein methylated As(III) to dimethylarsenate as the main product in the medium and also produced dimethylarsine and trimethylarsine gases. We propose that PaArsM plays a role in As methylation and detoxification of As(III) and could be exploited in bioremediation of As-contaminated environments.