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Volume 271, Number 30, Issue of July 26, 1996 pp. 17718-17723
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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A Salt-resistant Plasma Membrane Carbonic Anhydrase Is Induced by Salt in Dunaliella salina

(Received for publication, January 11, 1996, and in revised form, April 18, 1996)

From the Biochemistry Department, Weizmann Institute of Science, Rehovot 76100, Israel

The mechanisms allowing proliferation of the unicellular green alga Dunaliella salina in up to saturating NaCl concentrations are only partially understood at present. Previously, the level of a plasma membrane M_r 60,000 protein, p60, was found to increase with rising external salinities. Based on cDNA cloning and enzymatic assays, it is now shown that p60 is an internally duplicated carbonic anhydrase, with each repeat homologous to animal and Chlamydomonas reinhardtii carbonic anhydrases, but exceptional in the excess of acidic over basic residues. Increasing salinities, alkaline shift, or removal of bicarbonate induced in D. salina parallel increases in the levels of p60, its mRNA, and external carbonic anhydrase activity. Moreover, purified p60 exhibited carbonic anhydrase activity comparable to other carbonic anhydrases. A p60-enriched soluble preparation showed maximal carbonic anhydrase activity at ~1.0 M NaCl and retained considerable activity at higher salt concentrations. In contrast, a similar preparation from C. reinhardtii was ~90% inhibited in 0.6 M NaCl. These results identified p60 as a structurally novel carbonic anhydrase transcriptionally regulated by CO₂ availability and exhibiting halophilic-like characteristics. This enzyme is potentially suited to optimize CO₂ uptake by cells growing in hypersaline media.

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