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Vol. 273, Issue 3, 1727-1732, January 16, 1998
From the School of Biological Sciences, University of Auckland,
Private Bag 92019, Auckland, New Zealand
Ionic aluminum (Al3+) is toxic
to plants, microbes, fish, and animals, but the mechanism of its
toxicity is unknown. We describe the isolation of two yeast genes
(ALR1 and ALR2) which confer increased
tolerance to Al3+ and Ga3+ ions when
overexpressed while increasing strain sensitivity to Zn2+,
Mn2+, Ni2+, Cu2+, Ca2+,
and La3+ ions. The Alr proteins are homologous to the
Salmonella typhimurium CorA protein, a bacterial
Mg2+ and Co2+ transport system located in the
periplasmic membrane. Yeast strains lacking ALR gene
activity required additional Mg2+ for growth, and
expression of either ALR1 or ALR2 corrected the Mg2+-requiring phenotype. The results suggest that the
ALR genes encode the yeast uptake system for
Mg2+ and other divalent cations. This hypothesis was
supported by evidence that 57Co2+ accumulation
was elevated in ALR-overexpressing strains and reduced in
strains lacking ALR expression. ALR
overexpression also overcame the inhibition of Co2+ uptake
by Al3+ ions. The results indicate that aluminum toxicity
to yeast occurs as a consequence of reduced Mg2+ influx via
the Alr proteins. The molecular identification of the yeast
Mg2+ transport system should lead to a better understanding
of the regulation of Mg2+ homeostasis in eukaryote
cells.
Overexpression of the Saccharomyces cerevisiae
Magnesium Transport System Confers Resistance to Aluminum Ion
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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