Enhancement of Sensitivity in Aggregation-Based Whole-Cell Arsenite Sensor Utilizing Arsenic Metabolism Regulation
Chemistry
QD1-999
DOI:
10.1021/acsomega.4c11704
Publication Date:
2025-04-03T18:27:13Z
AUTHORS (10)
ABSTRACT
Arsenite [As(III)] is a toxic substance widely present on Earth, and the development of low-cost simple microbial-based As(III) sensors has been attracting attention. Recently, we discovered that protein LuxR, which contains multiple cysteine residues with high affinity for As(III), forms an insoluble structure upon binding to exhibits OFF-switching properties as quorum sensing transcriptional activator. Based this property, LuxR sensor operates new principle distinct from conventional whole-cell sensors; however, its sensitivity remains challenge. In study, aimed improve OFF-type by increasing frequency intracellular interactions between As(III). We utilized super-repressor ArsR, repressor As(III)-metabolizing ars operon, achieved replacing C34 in As(III)-binding domain Y. By linking ArsRC34Y constructed single plasmid create portable ArsRC34Y-LuxR protein. suppressing expression ArsB, efflux transporter encoded using ArsRC34Y, successfully enhanced response.
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