Flavoproteins are potential targets for the antibiotic roseoflavin in Escherichia coli.

Abstract:

: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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Langer S,Hashimoto M,Hobl B,Mathes T,Mack M

doi

10.1128/JB.00646-13

subject

Has Abstract

pub_date

2013-09-01 00:00:00

pages

4037-45

issue

18

eissn

0021-9193

issn

1098-5530

pii

JB.00646-13

journal_volume

195

pub_type

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