
TY  - JOUR
A1  - Matthijs, Hans C. P. 
A1  - Jeanjean, Robert 
A1  - Yeremenko, Nataliya 
A1  - Huisman, Jef 
A1  - Joset, Francoise 
A1  - Hellingwerf, Klaas J. 
T1  - Hypothesis: versatile function of ferredoxin-NADP<emph type="7">&#43;</emph> reductase in cyanobacteria provides regulation for transient photosystem I-driven cyclic electron flow
JF  - Functional Plant Biology
JO  - Functional Plant Biol.
Y1  - 2002
VL  - 29
IS  - 3
SP  - 201
EP  - 210
KW  - carbon dioxide fixation, cyanobacteria, ferredoxin-NADP&#43; reductase (FNR), NADH dehydrogenase type 1, photosynthesis, photosystem 1 cyclic electron transfer, salt stress, Synechocystis PCC6803.
UR  - https://doi.org/10.1071/PP01197 
N2  - Pseudo-reversion of the high-CO2 requiring phenotype of the NADH dehydrogenase type 1-impaired mutant of Synechocystis PCC6803, strain M55, by salt stress coincides with partial restoration of PSI-driven cyclic electron transfer. In M55, the complete family of D proteins (D1&#8211;D6) that are needed for electron transfer through the complex is lacking. Adaptation to salt stress requires de novo synthesis of full-length 47-kDa ferredoxin-NADP&#43; reductase (FNR). A mutant created in the M55 background, which only expresses truncated chloroplast 37-kDa FNR cannot adapt to salt stress and refrains from growth in low CO2. A special feature of FNR in cyanobacteria is the relatively high molecular mass of 44&#8211;48 kDa. A positively charged extended N-terminal domain of the cyanobacterial enzyme defines the extra mass. The extension likely plays a key role in the salt-stress inducible enhancement of PSI-driven cyclic electron transfer, and in the pseudo-reversion of the high-CO2 requiring phenotype of M55. Data acquired with several other cyanobacteria and the oxychlorobacterium Prochlorothrix hollandica contributed to the present hypothesis. It proposes that FNR is involved in regulation of inducible and transient PSI cyclic electron transfer in cyanobacteria via a thylakoid surface charge and conditional-proteolysis steered mechanism. 
ER  -

