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Plant and Cell Physiology, 2001, Vol. 42, No. 8 823-827
© 2001 Oxford University Press

Iron-Binding Activity of FutA1 Subunit of an ABC-type Iron Transporter in the Cyanobacterium Synechocystis sp. Strain PCC 6803

Hirokazu Katoh1, Natsu Hagino and Teruo Ogawa

Bioscience Center, Nagoya University, Chikusa, Nagoya, 464-8601 Japan

The futA1 (slr1295) and futA2 (slr0513) genes encode periplasmic binding proteins of an ATP-binding cassette (ABC)-type iron transporter in Synechocystis sp. PCC 6803. FutA1 was expressed in Escherichia coli as a GST-tagged recombinant protein (rFutA1). Solution containing purified rFutA1 and ferric chloride showed an absorption spectrum with a peak at 453 nm. The absorbance at this wavelength rose linearly as the amount of iron bound to rFutA1 increased to reach a plateau when the molar ratio of iron to rFutA1 became unity. The association constant of rFutA1 for iron in vitro was about 1x1019. These results demonstrate that the FutA1 binds the ferric ion with high affinity. The activity of iron uptake in the {Delta}futA1 and {Delta}futA2 mutants was 37 and 84%, respectively, of that in the wild-type and the activity was less than 5% in the {Delta}futA1/{Delta}futA2 double mutant, suggesting their redundant role for binding iron. High concentrations of citrate inhibited ferric iron uptake. These results suggest that the natural iron source transported by the Fut system is not ferric citrate.

1 Corresponding author: E-mail, L46611A@nucc.cc.nagoya-u.ac.jp; Fax, +81-52-789-5214.


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