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J. Biol. Chem., Vol. 275, Issue 27, 20551-20555, July 7, 2000

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Bicarbonate Binding Activity of the CmpA Protein of the Cyanobacterium Synechococcus sp. strain PCC 7942 Involved in Active Transport of Bicarbonate^*

Shin-ichi Maeda^§, G. Dean Price^§, Murray R. Badger^§, Chika Enomoto^¶, and Tatsuo Omata^¶

From the  Molecular Plant Physiology Group, Research School of Biological Sciences, Australian National University, P.O. Box 475, Canberra ACT 2601, Australia and the ^¶ Laboratory of Molecular Plant Physiology, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan

The cmpABCD operon of the cyanobacterium Synechococcus sp. strain PCC 7942 encodes an ATP-binding cassette transporter involved in HCO₃ uptake. The three genes, cmpBCD, encode membrane components of an ATP-binding cassette transporter, whereas cmpA encodes a 42-kDa cytoplasmic membrane protein, which is 46.5% identical to the membrane-anchored substrate-binding protein of the nitrate/nitrite transporter. Equilibrium dialysis analysis using H¹⁴CO₃ showed that a truncated CmpA protein lacking the N-terminal 31 amino acids, expressed in Escherichia coli cells as a histidine-tagged soluble protein, specifically binds inorganic carbon (CO₂ or HCO₃). The addition of the recombinant CmpA protein to a buffer caused a decrease in the concentration of dissolved CO₂ because of the binding of inorganic carbon to the protein. The decrease in CO₂ concentration was accelerated by the addition of carbonic anhydrase, indicating that HCO₃, but not CO₂, binds to the protein. Mass spectrometric measurements of the amounts of unbound and bound HCO₃ in CmpA solutions containing low concentrations of inorganic carbon revealed that CmpA binds HCO₃ with high affinity (K_d = 5 µM). A similar dissociation constant was obtained by analysis of the competitive inhibition of the CmpA protein on the carboxylation of phosphoenolpyruvate by phosphoenolpyruvate carboxylase at limiting concentrations of HCO₃. These findings showed that the cmpA gene encodes the substrate-binding protein of the HCO₃ transporter.

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