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XB-ART-9889
Microbiology (Reading) 2000 Dec 01;146 Pt 12:3251-3257. doi: 10.1099/00221287-146-12-3251.
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A functional water channel protein in the pathogenic bacterium Brucella abortus.

Rodrı Guez MAC , Froger A , Rolland JP , Thomas D , Agüero J , Delamarche C , Garcı A-Lobo JM .


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The gene for a new bacterial aquaporin, AqpX, was cloned from the pathogenic Gram-negative bacterium Brucella abortus. The gene was mapped on the large chromosome of B. abortus. It is flanked by one upstream and two downstream copies of the Brucella repeated sequence Bru-RS. Prediction from the nucleotide sequence indicated that the protein is a member of the MIP family, which comprises channels for water and/or solute transport. Expression in Xenopus oocytes and cryoelectron microscopy of Escherichia coli cells transformed with the aqpX gene confirmed that the protein is an efficient water channel. Glycerol uptake experiments in E. coli also showed that the protein is not able to transport glycerol.

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Species referenced: Xenopus
Genes referenced: mip