Open AccessIdentification and Characterization of a Fructose Phosphotransferase System in Bifidobacterium breve UCC2003
Author(s) -
Alain Mazé,
Mary O’Connell Motherway,
Gerald F. Fitzgerald,
Josef Deutscher,
Douwe van Sinderen
Publication year - 2007
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.01496-06
Subject(s) - operon , pep group translocation , biology , bacillus subtilis , bifidobacterium breve , in silico , complementation , genetics , gene , drosha , bifidobacterium longum , phosphoenolpyruvate carboxykinase , biochemistry , bifidobacterium , rna , bacteria , rna interference , escherichia coli , phenotype , lactobacillus
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.