Flavoproteins are potential targets for the antibiotic roseoflavin in Escherichia coli

Simone Langer, Masayuki Hashimoto, Birgit Hobl, Tilo Mathes, Matthias Mack

Research output: Contribution to journalArticlepeer-review

48 Citations (Scopus)


The riboflavin analog roseoflavin is an antibiotic produced by Streptomyces davawensis. Riboflavin transporters are responsible for roseoflavin uptake by target cells. Roseoflavin is converted to the flavin mononucleotide (FMN) analog roseoflavin mononucleotide (RoFMN) by flavokinase and to the flavin adenine dinucleotide (FAD) analog roseoflavin adenine dinucleotide (RoFAD) by FAD synthetase. In order to study the effect of RoFMN and RoFAD in the cytoplasm of target cells, Escherichia coli was used as a model. E. coli is predicted to contain 38 different FMN- or FAD-dependent proteins (flavoproteins). These proteins were overproduced in recombinant E. coli strains grown in the presence of sublethal amounts of roseoflavin. The flavoproteins were purified and analyzed with regard to their cofactor contents. It was found that 37 out of 38 flavoproteins contained either RoFMN or RoFAD. These cofactors have different physicochemical properties than FMN and FAD and were reported to reduce or completely abolish flavoprotein function.

Original languageEnglish
Pages (from-to)4037-4045
Number of pages9
JournalJournal of Bacteriology
Issue number18
Publication statusPublished - 2013

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology


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