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Fructose uptake in Bifidobacterium longum NCC2705 is mediated by an ATP-binding cassette transporter
Authors:Wei Xiao  Guo Yanhong  Shao Changlin  Sun Zhongke  Zhurina Daria  Liu Dawei  Liu Wei  Zou Dayang  Jiang Zheng  Wang Xuesong  Zhao Jiangli  Shang Wei  Li Xuelian  Liao Xiangru  Huang Liuyu  Riedel Christian U  Yuan Jing
Institution:Institute of Disease Control and Prevention, Academy of Military Medical Sciences, Beijing 100071, China.
Abstract:Recently, a putative ATP-binding cassette (ABC) transport system was identified in Bifidobacterium longum NCC2705 that is highly up-regulated during growth on fructose as the sole carbon source. Cloning and expression of the corresponding ORFs (bl0033-0036) result in efficient fructose uptake by bacteria. Sequence analysis reveals high similarity to typical ABC transport systems and suggests that these genes are organized as an operon. Expression of FruE is induced by fructose, ribose, or xylose and is able to bind these sugars with fructose as the preferred substrate. Our data suggest that BL0033-0036 constitute a high affinity fructose-specific ABC transporter of B. longum NCC2705. We thus suggest to rename the coding genes to fruEKFG and the corresponding proteins to FruE (sugar-binding protein), FruK (ATPase subunit), FruF, and FruG (membrane permeases). Furthermore, protein-protein interactions between the components of the transporter complex were determined by GST pulldown and Western blot analysis. This revealed interactions between the membrane subunits FruF and FruG with FruE, which in vivo is located on the external side of the membrane, and with the cytoplasmatic ATPase FruK. This is in line with the proposed model for bacterial ABC sugar transporters.
Keywords:ABC Transporter  Metabolism  Microbiology  Protein-Protein Interactions  Proteomics
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