Format

Send to

Choose Destination
Bioengineered. 2014;5(6):386-92. doi: 10.4161/21655979.2014.969173. Epub 2014 Nov 11.

YeeO from Escherichia coli exports flavins.

Author information

1
a Department of Chemical Engineering ; Pennsylvania State University; University Park , PA USA.

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.

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

PMID:
25482085
PMCID:
PMC4601484
DOI:
10.4161/21655979.2014.969173
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Taylor & Francis Icon for PubMed Central
Loading ...
Support Center