Primary structure and effect of pH on the expression of the plasma membrane H(+)-ATPase from Dunaliella acidophila and Dunaliella salina

Plant Physiology
M Weiss, U Pick

Abstract

The plasma membrane H(+)-ATPase gene was cloned and sequenced from the extremely acidophilic green alga Dunaliella acidophila and from the extremely halotolerant Dunaliella salina. A special feature of the Dunaliella H(+)-ATPase is an extended C-terminal domain. The deduced amino acid sequences of the two proteins are 75% identical but differ in their C terminus. A hydrophilic loop within this domain in D. salina, which presumably faces the cell exterior, has a high ratio of acidic over basic amino acids, typical of halophilic proteins. The amount of the ATPase protein in plasma membranes and the level of its mRNA transcript in D. acidophila are far higher than in D. salina, suggesting that D. acidophila overexpresses the enzyme. A pH shift from 9.0 to 7.0 induces in D. salina a large increase in the level of the H(+)-ATPase mRNA and in the amount of the H(+)-ATPase protein. This suggests that the expression of the H(+)-ATPase in D. salina is pH-regulated at the transcriptional level. The implications of these findings are discussed with respect to the adaptive pressures imposed on these algal species by their exceptional environmental conditions.

References

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Citations

Sep 17, 2005·Journal of Bioenergetics and Biomembranes·Javier Barrero-GilBegoña Benito
Jul 13, 2001·Plant Science : an International Journal of Experimental Plant Biology·I MaedaK Yagi
Feb 29, 2000·Biochimica Et Biophysica Acta·A Rodríguez-Navarro
Mar 6, 1999·Current Opinion in Plant Biology·D P DixonR Edwards
Mar 6, 1999·Current Opinion in Plant Biology·H J Bohnert, E Sheveleva
Mar 12, 2004·Annual Review of Plant Physiology and Plant Molecular Biology·Paul M. HasegawaHans J. Bohnert
Dec 2, 2009·Physiologia Plantarum·Barbara J Hawkins, Samantha Robbins
Jun 18, 2005·The Journal of Experimental Biology·Mark A MesserliMitchell L Sogin

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