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Involvement of photorespiration and glycolate pathway in carbonic anhydrase induction and inorganic carbon concentration in Chlamydomonas reinhardtii
Authors:Z. Ramazanov,J. Cá  rdenas
Affiliation:Inst. of Plant Physiology, Botanicheskaya 35, Academy of Sciences, Moscow 276, Russia;Departamentro de Bioquímica y Biología Molecular Y Fisiología, Facultad de Ciencias, Univ. de Córdoba, Avda. San Alberto Magno s/n, E-14071-Córdoba, Spain.
Abstract:Interaction between induction of carbonic anhydrase (CA) activity, induction of inorganic carbon (Ci) concentrating mechanisms and the photorespiratory glycolate pathway has been studied in wild type 6145c and photorespiratory mutant 18–7F (low in phosphoglycolate phosphatase activity) cells of C. reinhardtii . Cell transfer from high CO2 (5%, v/v) to low CO2 (0.03%) provoked an increase of extracellular and total (extracellular plus intracellular) CA in both wild type and mutant cells. During adaptation to low CO2 conditions, both strains excreted ammonium to the medium at a similar rate in the presence of l -methionine- d-l -sulfoximine (MSX), an inhibitor of glutamine synthetase (GS). MSX also provoked ammonium excretion by air adapted wild type and mutant cells, even though both strains had high levels of CA activity and of Ci concentrating activities.
GS increased in both strains after transfer from high to low CO2 conditions. However, this increase was abolished by aminooxyacetate, an inhibitor of the glyoxylate-serine aminotransferase, and by glycolaldehyde, an inhibitor of triose phosphate to ribulose 1,5-bisphosphate conversion. CA synthesis did not occur in the presence of either aminooxyacetate or glycolaldehyde. Algae grown in high CO2 in the presence of aminooxyacetate did not induce Ci concentrating mechanisms. Integration of these three processes, i.e., CA synthesis, Ci-concentration, and photorespiratory glycolate pathway is proposed in the framework of carbon metabolism of the alga.
Keywords:Carbonic anhydrase    Chlamydomonas reinhardtii    glycolate pathway    mutants
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