scholarly journals Identification and functional role of the carbonic anhydrase Cah3 in thylakoid membranes of pyrenoid of Chlamydomonas reinhardtii

2012 ◽  
Vol 1817 (8) ◽  
pp. 1248-1255 ◽  
Author(s):  
Maria A. Sinetova ◽  
Elena V. Kupriyanova ◽  
Alexandra G. Markelova ◽  
Suleyman I. Allakhverdiev ◽  
Natalia A. Pronina
FEBS Letters ◽  
1999 ◽  
Vol 444 (1) ◽  
pp. 102-105 ◽  
Author(s):  
Youn-Il Park ◽  
Jan Karlsson ◽  
Igor Rojdestvenski ◽  
Natalia Pronina ◽  
Viacheslav Klimov ◽  
...  

1986 ◽  
Vol 251 (5) ◽  
pp. G682-G687 ◽  
Author(s):  
A. N. Charney ◽  
J. D. Wagner ◽  
G. J. Birnbaum ◽  
J. N. Johnstone

We examined the role of carbonic anhydrase activity in intestinal transport by measuring the effect of systemic pH and PCO2 on electrolyte transport in the presence and absence of luminal acetazolamide. Adult Sprague-Dawley rats were anesthetized, and ileal and colonic segments were perfused with Ringer solution that was acetazolamide-free or that contained 0.1 mM sodium acetazolamide. Consecutive states of acute respiratory alkalosis and acidosis were created by changing the inspired CO2 from 0% (room air) to 8% CO2. In the ileum, acetazolamide perfusion did not affect the increment in net sodium and chloride absorption caused by a reduction in systemic pH. Mucosal carbonic anhydrase activity in this segment was measurable, although very low. In both the ascending and descending colon, acetazolamide perfusion reduced the increment in net sodium absorption caused by an increase in systemic PCO2. In addition, acetazolamide increased the chloride absorptive response to PCO2 in the ascending colon but did not affect the chloride response at all in the descending colon. Colonic mucosal carbonic anhydrase exhibited a proximal-to-distal gradient of activity: levels in the ascending colon were severalfold greater than in the descending colon. These findings suggest a functional role for carbonic anhydrase in mediating the colonic but not the ileal absorptive response to changes in systemic acid-base balance.


Channels ◽  
2011 ◽  
Vol 5 (2) ◽  
pp. 106-109 ◽  
Author(s):  
Hideomi Yamada ◽  
Shoko Horita ◽  
Masashi Suzuki ◽  
Toshiro Fujita ◽  
George Seki

2002 ◽  
Vol 29 (3) ◽  
pp. 243 ◽  
Author(s):  
Eddy van Hunnik ◽  
Dieter Sültemeyer

In order to understand the function of the lumen carbonic anhydrase (CA) which is bound to PSII at the lumenal side of the thylakoids in chloroplasts of eukaryotic algae, thylakoids were isolated from chloroplasts of Tetraedron minimum, Chlamydomonas noctigama, the cell wall-less mutant Chlamydomonas reinhardtii CW15, and a C. reinhardtii CW15/CIA3 mutant which lacks the lumen CA. The isolated thylakoids produced O2 on illumination and exhibited electron flow between PSII and PSI, indicating that the thylakoids were intact and the photosynthetic apparatus were functional. We could not detect any uptake of HCO3–,nor efflux of CO2, from the thylakoids upon illumination, making it improbable that the CA present in the lumen of the thylakoids would play a role in furnishing CO2 for Rubisco. We were able to determine ATP production upon illumination in isolated thylakoids. Under high inorganic carbon (Ci; 5 mM), all species showed significant amounts of ATP being produced. Under low Ci (200 M), we could not detect ATP formation from C. reinhardtii CW15/CIA3 upon illumination. This mutant was not able to survive more then 4 h of low Ci in culture. We therefore suggest that the lumen CA is not involved in the CO2 concentrating mechanism, but might play a role in the formation of a proton gradient across the thylakoid membranes.


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