Linked Life Data

20947511

Source:http://linkedlifedata.com/resource/pubmed/id/20947511

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pubmed-article:20947511pubmed:abstractTextSteady exposure to environmental arsenic has led to the evolution of vital cellular detoxification mechanisms. Under aerobic conditions, a two-step process appears most common among microorganisms involving reduction of predominant, oxidized arsenate (H(2)As(V)O(4)(-)/HAs(V)O(4)(2-)) to arsenite (As(III)(OH)(3)) by a cytosolic enzyme (ArsC; Escherichia coli type arsenate reductase) and subsequent extrusion via ArsB (E. coli type arsenite transporter)/ACR3 (yeast type arsenite transporter). Here, we describe novel fusion proteins consisting of an aquaglyceroporin-derived arsenite channel with a C-terminal arsenate reductase domain of phosphotyrosine-phosphatase origin, providing transposable, single gene-encoded arsenate resistance. The fusion occurred in actinobacteria from soil, Frankia alni, and marine environments, Salinispora tropica; Mycobacterium tuberculosis encodes an analogous ACR3-ArsC fusion. Mutations rendered the aquaglyceroporin channel more polar resulting in lower glycerol permeability and enhanced arsenite selectivity. The arsenate reductase domain couples to thioredoxin and can complement arsenate-sensitive yeast strains. A second isoform with a nonfunctional channel may use the mycothiol/mycoredoxin cofactor pool. These channel enzymes constitute prototypes of a novel concept in metabolism in which a substrate is generated and compartmentalized by the same molecule. Immediate diffusion maintains the dynamic equilibrium and prevents toxic accumulation of metabolites in an energy-saving fashion.lld:pubmed
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pubmed-article:20947511pubmed:authorpubmed-author:BeitzEricElld:pubmed
pubmed-article:20947511pubmed:authorpubmed-author:SongJieJlld:pubmed
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pubmed-article:20947511pubmed:year2010lld:pubmed
pubmed-article:20947511pubmed:articleTitleNovel channel enzyme fusion proteins confer arsenate resistance.lld:pubmed
pubmed-article:20947511pubmed:affiliationDepartment of Pharmaceutical and Medicinal Chemistry, Christian-Albrechts-Universität zu Kiel, 24118 Kiel, Germany.lld:pubmed
pubmed-article:20947511pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:20947511pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed