Regulation and Function of Lysine-Substituted Na,K Pumps in Salt Adaptation of Artemia franciscana

Regulation and Function of Lysine-Substituted Na,K Pumps in Salt Adaptation of Artemia franciscana The brine shrimp Artemia thrives at extreme conditions of up to 300 g/l salt in hypersaline lakes, but the molecular aspects of this salt adaptation are not clarified. To examine the influence of salt on the expression of two isoforms of Na,K-ATPase, adult Artemia franciscana were cultured for 39 days with the microalga Dunaliella salina as fodder at increasing salt from 30 to 280 g/l. Quantitative reverse-transcriptase polymerase chain reaction showed that the abundance of mRNA of the lysine-substituted α2(KK)-subunit was very low at 30 g/l salt but rose steeply in the range of 70–200 g/l to a level at 200–280 g/l salt, similar to the abundance of the mRNA of the α1(NN)-subunit, which was insignificantly affected by increasing salt. Site-directed mutagenesis showed that Asn324Lys and Asn776Lys in the α1-subunit of pig kidney Na,K-ATPase reduced the stoichiometry of 204Tl binding from 2 to about 1 Tl+(K+) per α-subunit and Na+-dependent phosphorylation from ATP to 25–30%. In structure models, the ε-amino group of Lys776 is located at cation site 1 in the E1P form and near cation site 2 in the E2 conformation, while the side chain of Lys324 points away from the cation sites. Salt-induced expression of the α2(KK)-subunit Na,K-ATPase in A. franciscana may reduce the Na+/ATP ratio and enable the Na,K pump to extrude Na+ against steeper gradients and, thus, contribute to salt adaptation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Regulation and Function of Lysine-Substituted Na,K Pumps in Salt Adaptation of Artemia franciscana

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Publisher
Springer-Verlag
Copyright
Copyright © 2007 by Springer Science+Business Media, LLC
Subject
Life Sciences; Human Physiology ; Biochemistry, general
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s00232-007-9083-3
Publisher site
See Article on Publisher Site

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