Arsenic Methylation and Volatilization by Arsenite S -Adenosylmethionine Methyltransferase in Pseudomonas alcaligenes NBRC14159
Author(s) -
Jun Zhang,
Tingting Cao,
Zhu Tang,
Qirong Shen,
Barry P. Rosen,
FangJie Zhao
Publication year - 2015
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.03804-14
Subject(s) - arsenite , methylation , methyltransferase , alcaligenes faecalis , alcaligenes , arsenic , biotransformation , pseudomonas , microbiology and biotechnology , escherichia coli , biochemistry , biology , heterologous expression , chemistry , enzyme , bacteria , gene , genetics , organic chemistry , recombinant dna
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.
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