4.5 Article

Structure, function and regulation of the cyanobacterial high-affinity bicarbonate transporter, BCT1

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FUNCTIONAL PLANT BIOLOGY
卷 29, 期 2-3, 页码 151-159

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CSIRO PUBLISHING
DOI: 10.1071/PP01215

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ABC transporter; bicarbonate transporter; CO2 concentrating mechanism; cyanobacteria

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The cmpABCD operon of the cyanobacterium Synechococcus sp. strain PCC7942, which is transcribed specifically under CO2-limited growth conditions, encodes an (A) under bar TP-(b) under bar inding (c) under bar assette (ABC) transporter involved in HCO3- uptake (designated BCT1). The product of the cmpA gene is a 42-kDa protein anchored to the plasma membrane, which binds HCO3- with high affinity (K-d = 5 muM) and acts as the substrate-binding protein of the transporter. The apparent K-m(HCO3-) of BCT 1 is 15 muM. BCT 1 has the highest affinity for HCO3- among the HCO3- transporters of the Synechococcus strain and is essential for competitive utilization of HCO3- under CO2-limited conditions. BCT 1 is closely related to the cyanobacterial nitrate/nitrite transporter (NRT) encoded by the nrtABCD genes. The BCT1 and NRT transporters, together with the putative cyanate transporter of cyanobacteria, comprise a monoanion transporter subfamily in the family of ABC importers. BCT1 and NRT are present in most fresh-water strains of cyanobacteria but seem to be absent in marine cyanobacterial strains. The low CO2-responsive induction of the cmp operon requires a LysR family protein CmpR, which is similar to CbbR (RbcR), the activator of the CO2 fixation operons of chemoautotrophic and purple photosynthetic bacteria.

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