Yeeo from Escherichia coli exports flavins

Michael J. McAnulty, Thomas K. Wood

Research output: Contribution to journalArticle

21 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)386-392
Number of pages7
JournalBioengineered Bugs
Volume5
Issue number6
DOIs
StatePublished - Nov 11 2014

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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