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Microbiology 146 (2000), 3251-3257
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Microbiology (2000), 146, 3251-3257.
© 2000 Society for General Microbiology


Bioenergetics and Transport

A functional water channel protein in the pathogenic bacterium Brucella abortus

María C. Rodríguez1, Alexandrine Froger2, Jean-Paul Rolland2, Daniel Thomas2, Jesús Agüero1, Christian Delamarche2 and Juan M. García-Lobo1

Departamento de Biología Molecular, Facultad de Medicina, Universidad de Cantabria, Unidad asociada al Centro de Investigaciones Biológicas, CSIC, Cardenal Herrera Oria s/n, 39011 Santander, Spain1
UPRES-A CNRS 6026, Biologie Cellulaire et Reproduction, Equipe Canaux et Récepteurs Membranaires, Université de Rennes 1, Campus de Beaulieu, 35042 Rennes cedex, Bretagne, France2

Author for correspondence: Juan M. García-Lobo. Tel: +34 942 201948. Fax: +34 942 201945. e-mail: jmglobo{at}unican.es

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.

Keywords: aquaporin, water channel, Brucella abortus

The GenBank accession number for the nucleotide sequence reported in this paper is AF148066.




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