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Splice-variant 1 of the ancient domain protein 2 (ACDP2) complements the magnesium-deficient growth phenotype of Salmonella enterica sv. typhimurium strain MM281 Volume 23, numéro 2, June 2010

Auteurs
Max F. Perutz Laboratories, Department of Microbiology, Immunobiology and Genetics, Campus Vienna Biocenter, University of Vienna, Wien, Austria, FBN Dummerstorf, Institute of Nutritional-Physiology, Dummerstorf, Institute of Prevention and Nutrition, Ismaning, Institute of Veterinary-Physiology, Free University Berlin, Berlin, Germany

Evidence arguing for the existence of genes encoding for proteins directly involved in the transport of Mg 2+ through the cytoplasmic membrane have accumulated over the last few years. Gene ACDP2 (ancient conserved domain protein 2; old name CNNM2, cyclin M2) is one such gene. ACDP2 is a distant homologue of the bacterial gene corC, which is known to be involved in cobalt resistance. We have previously demonstrated that the over-expression of the human Mg 2+ carrier SLC41A1 partly complements the Mg 2+-dependent growth deficiency of Salmonella strain MM281 (triple disruptant in genes: mgtA, mgtB and corA) cultivated in media containing growth non-permissive [Mg 2+] e. We have used the same approach to examine whether over-expressed human ACDP2 has a similar efficacy to complement growth deficiency of the MM281 strain in media containing growth non-permissive [Mg 2+] e. Two splicing variants of the ACDP2 gene have been tested. Here, we show that over-expressed isomorph 1 is efficient in restoring growth of the MM281 strain in media containing growth non-permissive [Mg 2+] e, whereas isomorph 2 is not. Therefore, we conclude that ACDP2sp.v.1 is a functional Mg 2+-transporting entity per se. Our conclusion is supported by the measurable Mg 2+ influx seen in MM281 bacteria over-expressing ACDP2sp.v.1 but not in MM281 bacteria over-expressing ACDP2sp.v.2 or in cells transformed with the empty vector.