Carbonic anhydrase in eukaryotic algae: characterization, regulation, and possible function during photosynthesis

1998 ◽  
Vol 76 (6) ◽  
pp. 962-972 ◽  
Author(s):  
Dieter Sültemeyer

Carbonic anhydrase (CA) speeds up the equilibrium between CO2 and HCO3- at physiological pH values and has been detected in almost every species of the animal and plant kingdoms. Among eucaryotic micro- and macro-algae the enzyme is widely distributed and plays an important role in photosynthetic CO2 fixation. In some cases, different forms of carbonic anhydrases located extracellularly and intracellularly have been found to occur in the same cell. The expression of the genes encoding these CA isoforms are under the control of the inorganic carbon concentration in the medium, as the activities increase with decreasing the inorganic carbon content. Considerable progress has been made in recent years in isolating and characterizing the various forms of carbonic anhydrases on a biochemical and molecular level. Most of the data have been collected for microalgae like Chlamydomonas reinhardtii (Dangeard), while the situation in macroalgae is still descriptive. Therefore, this review summarizes the recent development with an emphasis on microalgae carbonic anhydrases.Key words: carbonic anhydrase, CO2 concentrating mechanism, macroalgae, microalgae, photosynthesis.

2002 ◽  
Vol 29 (3) ◽  
pp. 183 ◽  
Author(s):  
Anthony K.-C. So ◽  
Swan S.-W. Cot ◽  
George S. Espie

Sequence analysis of the carboxysomal carbonic anhydrase (CcaA) from Synechocystis PCC6803, Synechococcus PCC7942 and Nostoc ATCC29133, indicated high sequence identity to the β class of plant and bacterial carbonic anhydrases (CA), and conservation of the active site region. However, the cyanobacterial enzyme has a C-terminal extension of about 75 amino acids (aa) not found in the plant enzymes, and largely absent from other bacterial enzymes. Using recombinant DNA technology, genes encoding C-terminal truncation products of up to 127 aa were overexpressed in E. coli, and partially purified lysates were analysed for CA-mediated exchange of 18O between 13C18O2and H216O. Recombinant CcaA proteins with up to 60 aa removed (CcaAΔ60) were catalytically competent, but beyond this there was an abrupt loss of activity. CcaAΔ0, along with CcaAΔ40 and CcaAΔ60, also catalysed the hydrolysis of carbon oxysulfide (COS; an isoelectronic structural analogue of CO2), but CcaAΔ63 and CcaAΔ127 did not, indicating that truncations greater than 62 aa resulted in a general loss of catalytic competency. Analysis of protein-protein interaction using the yeast two-hybrid system revealed that CcaA did not interact with the large or small Rubisco subunits (RbcL and RbcS, respectively) of Synechocystis, but there was strong CcaA-CcaA interaction. This protein interaction also ceased with C-terminal truncations in CcaA greater than 60 aa. The correlation between loss of CcaA-CcaA interaction and CcaA catalytic activity suggests that the proximal portion of the C-terminal extension is required for oligomerization, and that this oligomerization is essential for catalysis by the cyanobacterial enzyme. Thus, the C-terminal extension may play an important role in the function of CA within cyanobacterial carboxysomes, which is not required by the higher plant enzymes.


Sign in / Sign up

Export Citation Format

Share Document