Fast Induction of High-Affinity HCO₃ Transport in Cyanobacteria¹

Dieter Sültemeyer^*, Barbara Klughammer, Murray R. Badger, and G. Dean Price

Fachbereich Biologie, Universität Kaiserslautern, Postfach 3049, D-67653 Kaiserslautern, Germany (D.S.); Julius-von-Sachs-Institut für Biowissenschaften, Universität Würzburg, Mittlerer Dallenbergweg 64, D-97082 Würzburg, Germany (B.K.); and Molecular Plant Physiology Group, Research School of Biological Sciences, Australian National University, P.O. Box 475, Canberra, ACT 0200, Australia (M.R.B., G.D.P.)

The induction of a high-affinity state of the CO₂-concentration mechanism was investigated in two cyanobacterial species, Synechococcus sp. strain PCC7002 and Synechococcus sp. strain PCC7942. Cells grown at high CO₂ concentrations were resuspended in low-CO₂ buffer and illuminated in the presence of carbonic anhydrase for 4 to 10 min until the inorganic C compensation point was reached. Thereafter, more than 95% of a high-affinity CO₂-concentration mechanism was induced in both species. Mass-spectrometric analysis of CO₂ and HCO₃ fluxes indicated that only the affinity of HCO₃ transport increased during the fast-induction period, whereas maximum transport activities were not affected. The kinetic characteristics of CO₂ uptake remained unchanged. Fast induction of high-affinity HCO₃ transport was not inhibited by chloramphenicol, cantharidin, or okadaic acid. In contrast, fast induction of high-affinity HCO₃ transport did not occur in the presence of K252a, staurosporine, or genistein, which are known inhibitors of protein kinases. These results show that induction of high-affinity HCO₃ transport can occur within minutes of exposure to low-inorganic-C conditions and that fast induction may involve posttranslational phosphorylation of existing proteins rather than de novo synthesis of new protein components.

Plant Physiol. (1998) 116: 183-192
Copyright Clearance Center:   0032-0889/98/116/0183/10
© 1998 American Society of Plant Physiologists

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