Interrelation between Cyanophycin Synthesis, L-Arginine Catabolism and Photosynthesis in the Cyanobacterium Synechocystis Sp. Strain PCC 6803

2000 ◽  
Vol 55 (11-12) ◽  
pp. 927-942 ◽  
Author(s):  
Dirk Paul Stephan ◽  
Hans Georg Ruppel ◽  
Elfriede K. Pistorius

ʟ Ultrastructural and imm unocytochemical investigations gave evidence that cyanophycin (multi--arginyl-poly-ʟ-aspartate) granules accumulate in the cyanobacterium Synechocystis sp. strain PCC 6803 under nutrient deficient growth conditions, especially under phosphate limitation. Besides nutrient deficiency, growth of Synechocystis PCC 6803 on ʟ-arginine or ʟ-asparagine as sole N-source also led to high increase of cyanophycin synthesis, while growth on the combination of ʟ-arginine or ʟ-asparagine with nitrate only caused minor cyanophycin accum ulation. Growth of Synechocystis PCC 6803 on ʟ-arginine as sole N-source caused substantial morphological and physiological changes, such as severe thylakoid membrane degradation with partial loss of pigments and photosynthetic activity leading to a phenotype almost like that seen under nutrient deficiency. In contrast to the wild type, the PsbO-free Synechocystis PCC 6803 mutant could grow on ʟ-arginine as sole N-source with only minor morphological and physiological changes. Due to its fairly balanced growth, the mutant accumulated only few cyanophycin granules. ʟ-arginine degrading activity (measured as ornithine and ammonium formation) was high in the PsbO-free mutant but not in the wild type when cells were grown on ʟ-arginine as sole N-source. In both cells types the ʟ-arginine degrading activity was high (although in the PsbO-free mutant about twice as high as in wild type), when cells were grown on ʟ-arginine in combination with nitrate, and as expected very low when cells were grown on nitrate as sole N-source. Thus, net cyanophycin accumulation in Synechocystis PCC 6803 is regulated by the relative concentration of ʟ-arginine to the total nitrogen pool, and the intracellular ʟ-arginine concentration is greatly influenced by the activity of the ʟ-arginine degrading enzyme system which in part is regulated by the activity status of photosystem II. These results suggest a complex interrelation between cyanophycin synthesis, ʟ-arginine catabolism , and in addition photosynthesis in Synechocystis PCC 6803.

2016 ◽  
Vol 81 (8) ◽  
pp. 858-870
Author(s):  
O. V. Voloshina ◽  
Y. V. Bolychevtseva ◽  
F. I. Kuzminov ◽  
M. Y. Gorbunov ◽  
I. V. Elanskaya ◽  
...  

2004 ◽  
Vol 186 (23) ◽  
pp. 8144-8148 ◽  
Author(s):  
Terry M. Bricker ◽  
Shulu Zhang ◽  
Susan M. Laborde ◽  
Paul R. Mayer ◽  
Laurie K. Frankel ◽  
...  

ABSTRACT A mutation was recovered in the slr0721 gene, which encodes the decarboxylating NADP+-dependent malic enzyme in the cyanobacterium Synechocystis sp. strain PCC 6803, yielding the mutant 3WEZ. Under continuous light, 3WEZ exhibits poor photoautotrophic growth while growing photoheterotrophically on glucose at rates nearly indistinguishable from wild-type rates. Interestingly, under diurnal light conditions (12 h of light and 12 h of dark), normal photoautotrophic growth of the mutant is completely restored.


2018 ◽  
Vol 15 (4) ◽  
pp. 320-328 ◽  
Author(s):  
Chunsheng Xie ◽  
Xiange Wu ◽  
Jie Zhao ◽  
Xinhua Xu ◽  
Jianwen Hu ◽  
...  

2012 ◽  
Vol 78 (17) ◽  
pp. 6349-6351 ◽  
Author(s):  
Lawrence E. Page ◽  
Michelle Liberton ◽  
Himadri B. Pakrasi

ABSTRACTTruncation of the algal light-harvesting antenna is expected to enhance photosynthetic productivity. The wild type and three mutant strains ofSynechocystissp. strain 6803 with a progressively smaller phycobilisome antenna were examined under different light and CO2conditions. Surprisingly, such antenna truncation resulted in decreased whole-culture productivity for this cyanobacterium.


1993 ◽  
Vol 48 (3-4) ◽  
pp. 224-233 ◽  
Author(s):  
V. A. Boichenko ◽  
V. V. Klimov ◽  
S. R. Mayes ◽  
J. Barber

Abstract The absence of the extrinsic Mn-stabilizing 33 kDa protein in the IC 2 mutant of Synechocystis PCC 6803 disturbs the redox cycling of the water splitting system and retards the formation of its higher S-states (I. Vass, K. Cook, S. Deak, S. R. Mayes, and J. Barber, Biochim. Biophys. Acta 1102, 195-201 (1992)). We have performed analyses of the flashinduced oxygen exchange in the mutated cyanobacterium to clarify further the role of the 33 kDa protein. Under aerobic conditions, both the wild type and IC2 mutant show a relatively slow signal of oxygen rise on the first flash which is increased about twice by the addition of 10 μᴍ DCMU and significantly diminished by lowering the oxygen concentration in the medium. According to action spectra measurements, this mode of apparent oxygen release is mediated by PS I and can be attributed to a light induced inhibition of respiratory activity. In contrast to the wild type, having the usual oxygen evolution flash pattern with a periodicity of four, the IC2 mutant shows a binary oscillation pattern of flash-induced respiratory oxygen exchange at a flash frequency 10 Hz, being dampened with DCMU or by a lower flash frequency (< 1 Hz). Oxygen evolution due to water splitting is clearly seen in the IC2 mutant when background far-red illumination is applied to saturate the signal due to respiratory inhibition, but a quadruple oscillatory component of flash-induced oxygen evolution appears only in the presence of artificial electron acceptors under partial aerobic conditions. The mutant possesses a higher PS I/PS II ratio compared to the wild type, as judged from both the flashinduced yields and quantum efficiencies of the steady-state rates of the oxygen exchange reactions. Estimates of antenna sizes indicate about a 20% decrease of optical cross-section at 675 nm of the PS II unit in IC2 mutants in comparison with the wild type. It is suggested that the absence of the 33 kDa protein leads to a modification of the PS II assembly and because of the slowing down of the S-state cycle, the rate of cyclic electron flow around PS II is enhanced. It seems that the absence of the 33 kDa protein in Synechocystis 6803 also disturbs energy transfer between adjacent PS II core complexes and may also alter their association with the phycobilisomes.


2006 ◽  
Vol 188 (20) ◽  
pp. 7306-7310 ◽  
Author(s):  
Devaki Bhaya ◽  
Kenlee Nakasugi ◽  
Fariba Fazeli ◽  
Matthew S. Burriesci

ABSTRACT We have carefully characterized and reexamined the motility and phototactic responses of Synechocystis sp. adenylyl cyclase (Cya1) and catabolite activator protein (SYCRP1) mutants to different light regimens, glucose, 3-(3,4-dichlorophenyl)-1,1-dimethylurea, and cyclic AMP. We find that contrary to earlier reports, cya1 and sycrp1 mutants are motile and phototactic but are impaired in one particular phase of phototaxis in comparison with wild-type Synechocystis sp.


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