| Literature DB >> 25482085 |
Michael J McAnulty1, Thomas K Wood.
Abstract
Multidrug and toxic compound extrusion (MATE) proteins help maintain cellular homeostasis by secreting metabolic wastes. Flavins may occur as cellular waste products, with their production and secretion providing potential benefit for industrial applications related to biofuel cells. Here we find that MATE protein YeeO from Escherichia coli exports both flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). Significant amounts of flavins were trapped intracellularly when YeeO was produced indicating transport limits secretion of flavins. Wild-type E. coli secreted 3 flavins (riboflavin, FMN, and FAD), so E. coli likely produces additional flavin transporters.Entities:
Keywords: FAD, Flavin adenine dinucleotide; FMN, Flavin mononucleotide; IPTG, Isopropyl β-D-1-thiogalactopyranoside; LB, Lysogeny Broth; M9-glc, M9 minimal media supplemented with 0.4% glucose; M9-glc-caa, M9 minimal media supplemented with 0.4% glucose and 0.4% casamino acids; MATE, multidrug and toxic efflux; PVDF, Polyvinylidene fluoride; flavin; flavin adenine dinucleotide; flavin mononucleotide; transporter
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Year: 2014 PMID： 25482085 PMCID： PMC4601484 DOI： 10.4161/21655979.2014.969173
Source DB: PubMed Journal: Bioengineered ISSN： 2165-5979 Impact factor: 3.269