Identification and characterization of a fructose phosphotransferase system in Bifidobacterium breve UCC2003

  • Alain Mazé
  • , Mary O'Connell-Motherway
  • , Gerald F. Fitzgerald
  • , Josef Deutscher
  • , Douwe Van Sinderen

Research output: Contribution to journalArticlepeer-review

Abstract

In silico analysis of the Bifidobacterium breve UCC2003 genome allowed identification of four genetic loci, each of which specifies a putative enzyme II (EII) protein of a phosphoenolpyruvate:sugar phosphotransferase system. The EII encoded by fruA, a clear homologue of the unique EIIBCA enzyme encoded by the Bifidobacterium longum NCC2705 genome, was studied in more detail. The fruA gene is part of an operon which contains fruT, which is predicted to encode a homologue of the Bacillus subtilis antiterminator LicT. Transcriptional analysis showed that the fru operon is induced by fructose. The genetic structure, complementation studies, and the observed transcription pattern of the fru operon suggest that the EII encoded in B. breve is involved in fructose transport and that its expression is controlled by an antiterminator mechanism. Biochemical studies unequivocally demonstrated that FruA phosphorylates fructose at the C-6 position.

Original languageEnglish
Pages (from-to)545-553
Number of pages9
JournalApplied and Environmental Microbiology
Volume73
Issue number2
DOIs
Publication statusPublished - Jan 2007

Fingerprint

Dive into the research topics of 'Identification and characterization of a fructose phosphotransferase system in Bifidobacterium breve UCC2003'. Together they form a unique fingerprint.

Cite this