Show simple item record

dc.contributor.authorLiu, Guanghui
dc.contributor.authorLiu, Mengyao
dc.contributor.authorKim, Eun-Hae
dc.contributor.authorMaaty, Walid S.
dc.contributor.authorBothner, Brian
dc.contributor.authorLei, Benfang
dc.contributor.authorRensing, Christopher
dc.contributor.authorWang, Gejiao
dc.contributor.authorMcDermott, Timothy R.
dc.date.accessioned2016-06-23T17:01:20Z
dc.date.available2016-06-23T17:01:20Z
dc.date.issued2011-12
dc.identifier.citationLiu, Guanghui, Mengyao Liu, Eun-Hae Kim, Walid S. Maaty, Brian Bothner, Benfang Lei, Christopher Rensing, Gejiao Wang, and Timothy R. McDermott. “A Periplasmic Arsenite-Binding Protein Involved in Regulating Arsenite Oxidation.” Environmental Microbiology 14, no. 7 (December 19, 2011): 1624–1634. doi:10.1111/j.1462-2920.2011.02672.x.en_US
dc.identifier.issn1462-2912
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/9905
dc.description.abstractArsenic (As) is the most common toxic element in the environment, ranking first on the Superfund List of Hazardous Substances. Microbial redox transformations are the principal drivers of As chemical speciation, which in turn dictates As mobility and toxicity. Consequently, in order to manage or remediate environmental As, land managers need to understand how and why microorganisms react to As. Studies have demonstrated a two-component signal transduction system comprised of AioS (sensor kinase) and AioR (response regulator) is involved in regulating microbial AsIII oxidation, with the AsIII oxidase structural genes aioB and aioA being upregulated by AsIII. However, it is not known whether AsIII is first detected directly by AioS or by an intermediate. Herein we demonstrate the essential role of a periplasmic AsIII-binding protein encoded by aioX, which is upregulated by AsIII. An ΔaioX mutant is defective for upregulation of the aioBA genes and consequently AsIII oxidation. Purified AioX expressed without its TAT-type signal peptide behaves as a monomer (MW 32 kDa), and Western blots show AioX to be exclusively associated with the cytoplasmic membrane. AioX binds AsIII with a KD of 2.4 µM AsIII; however, mutating a conserved Cys108 to either alanine or serine resulted in lack of AsIII binding, lack of aioBA induction, and correlated with a negative AsIII oxidation phenotype. The discovery and characterization of AioX illustrates a novel AsIII sensing mechanism that appears to be used in a range of bacteria and also provides one of the first examples of a bacterial signal anchor protein.en_US
dc.titleA periplasmic arsenite-binding protein involved in regulating arsenite oxidationen_US
dc.typeArticleen_US
mus.citation.extentfirstpage1624en_US
mus.citation.extentlastpage1634en_US
mus.citation.issue7en_US
mus.citation.journaltitleEnvironmental Microbiologyen_US
mus.citation.volume14en_US
mus.identifier.categoryHealth & Medical Sciencesen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1111/j.1462-2920.2011.02672.xen_US
mus.relation.collegeCollege of Agricultureen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.universityMontana State University - Bozemanen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record