Photoinhibition and Recovery of Photosynthesis in <i>psbA</i> Gene-Inactivated Strains of Cyanobacterium <i>Anacystis nidulans</i>

Krupa, Zbigniew; Öquist, Gunnar; Gustafsson, Petter

doi:10.1104/pp.93.1.1

Cited by 45 publications

(37 citation statements)

References 23 publications

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“…When the rate of damage exceeds that of synthesis of new D1 subunits, photoinhibition results (42,43,52,58). The changes in psbA and psbD expression and in PSII protein synthesis and turnover match well with predictions based on a need for increased synthesis of the reaction center subunits at high light (6,31,32). It is not yet clear whether the blue/red and low/high-light responses of the psbA family in Synechococcus sp.…”

supporting

confidence: 52%

Light-responsive gene expression in cyanobacteria

Golden

1995

J Bacteriol

123

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supporting

confidence: 52%

Light-responsive gene expression in cyanobacteria

Golden

1995

J Bacteriol

123

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“…In addition, low temperature is thought to reduce rates of diffusion, removal, and degradation of damaged reaction PSII centers (10,11,19). Diffusion limitation of this repair cycle by low temperatures is supported by data showing that migration of the apoprotein of the oligomeric form of the light-harvesting complex associated with PSII from the stroma to the grana is blocked at 100C in barley thylakoids (32).…”

Section: Atrazine Bindingmentioning

confidence: 97%

Effect of Cold Hardening on Sensitivity of Winter and Spring Wheat Leaves to Short-Term Photoinhibition and Recovery of Photosynthesis

Hurry¹,

Hüner²

1992

Plant Physiol.

111

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Photoinhibition of photosynthesis and its recovery were studied in wheat (Triticum aestivum L.) leaves grown at nonhardening (20°C) and cold-hardening (5°C) temperatures. Cold-hardened wheat leaves were less susceptible to photoinhibition at 5°C than nonhardened leaves, and the winter cultivars, Kharkov and Monopol, were less susceptible than the spring cultivar, Glenlea. The presence of chloramphenicol, a chloroplastic protein synthesis inhibitor, increased the susceptibility to photoinhibition, but coldhardened leaves still remained less susceptible to photoinhibition than nonhardened leaves. Recovery at 50 Mmol m-2 S-1 photosynthetic photon flux density and 20°C was at least biphasic, with a fast and a slow phase in all cultivars. Cold-hardened leaves recovered maximum fluorescence and maximum variable fluorescence in the dark-adapted state during the fast phase at a rate of 42% h-' compared with 22% h-1 for nonhardened leaves. The slow phase occurred at similar rates (2% h-') in cold-hardened and nonhardened leaves. Full recovery required up to 30 h. Fastrecovery phase was not reduced by either lowering the recovery temperature to 50C or by the presence of chloramphenicol. Slowrecovery phase was inhibited by both treatments. Hence, the fast phase of recovery does not require de novo chloroplast protein synthesis. In addition, only approximately 60% of the photochemical efficiency lost through photoinhibition at 5C was associated with lost [14C]atrazine binding and, hence, with damage to the secondary quinone electron acceptor for photosystem II-binding site. We conclude that the decrease in susceptibility to photoinhibition exhibited following cold hardening of winter and spring cultivars is not due to an increased capacity for repair of photoinhibitory damage at 5°C but reflects intrinsic properties of the cold-hardened photosynthetic apparatus. A model to account for the fast component of recovery is discussed.Cold-tolerant cereals such as winter wheat (Triticum aestivum L.) and winter rye (Secale cereale L.) acquire maximum freezing tolerance following prolonged growth and development of seedlings at low, nonfreezing temperatures (0-50C) (18,21 more, damage to the photosynthetic apparatus, typically first expressed as photoinhibition, is exacerbated when high irradiance accompanies the low-temperature exposure (25,27). Typically, plants with larger antenna, such as shade plants (1), or plants with limited potential to fix CO2, such as plants exposed to low temperatures (25, 28), exhibit increased susceptibility to photoinhibition. Photoinhibition reduces the photochemical efficiency of PSII and it is typically detected as a decrease in FV3, Fv/FM, or a decrease in the quantum yield of 02 evolution (4, 14, 17).Greer et al. (10) suggested that the susceptibility of barley (Hordeum vulgare L.) to low-temperature-induced photoinhibition is due to an imbalance between rates of damage and repair of PSII reaction center polypeptides through de novo chloroplastic protein synthesis. However, winter rye (20...

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“…Synechococcus sp. PCC 7942 and the two psbA gene-inactivated mutants (strains R2S2C3 and R2K1) described by Golden et al (4) were grown in batch cultures in an inorganic medium (13 (14).…”

Section: Methodsmentioning

confidence: 99%

Two functionally distinct forms of the photosystem II reaction-center protein D1 in the cyanobacterium Synechococcus sp. PCC 7942.

Clarke

Hurry

Gustafsson

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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The cyanobacterium Synechococcus sp. PCC 7942 possesses a small psbA multigene family that codes for two distinct forms of the photosystem II reaction-center protein Dl (D1:1 and D1:2). We showed previously that the normally predominant Dl form (D1:1) was rapidly replaced with the alternative D1:2 when cells adapted to a photon irradiance of 50 pmol mM2's'1 are shifted to 500 ,umol m-2 s-1 and that this interchange was readily reversible once cells were allowed to recover under the original growth conditions. By using thepsbA inactivation mutants R2S2C3 and R2K1 (which synthesize only D1:1 and D1:2, respectively), we showed that this interchange between Dl forms was essential for limiting the degree of photoinhibition as well as enabling a rapid recovery of photosynthesis. In this report, we have extended these findings by examining whether any intrinsic functional differences exist between the two Dl forms that may afford increased resistance to photoinhibition. Initial studies on the rate of Dl degradation at three photon irradiances (50, 200, and 500 #mol'm-2 s'1) showed that the rates ofdegradation for both Dl forms increase with increasing photon flux density but that there was no signiicant difference between Dl:1 and D1:2. Analysis of light-response curves for oxygen evolution for the mutants R2S2C3 and R2K1 revealed that cells with photosystem II reaction centers containing D1:2 have a higher apparent quantum yield (=25%) than cells possessing D1:1. Further studies using chlorophyll a fluorescence measurements confirmed that R2K1 has a higher photochemical yield than R2S2C3; that is, a more efficient conversion of excitation energy from photon absorption into photochemistry. We believe that the higher photochemical efficiency of reaction centers containing D1:2 is causally related to the preferential induction of D1:2 at high light and thus may be an integral component of the protection mechanism within Synechococcus sp. PCC 7942 against photoinhibition.The reaction center of photosystem II (PSII) consists of two structurally similar proteins, Dl and D2, as well as cytochrome b559 and the psbl gene product (for a recent review, see ref.

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Photoinhibition and Recovery of Photosynthesis in psbA Gene-Inactivated Strains of Cyanobacterium Anacystis nidulans

Cited by 45 publications

References 23 publications

Light-responsive gene expression in cyanobacteria

Light-responsive gene expression in cyanobacteria

Effect of Cold Hardening on Sensitivity of Winter and Spring Wheat Leaves to Short-Term Photoinhibition and Recovery of Photosynthesis

Two functionally distinct forms of the photosystem II reaction-center protein D1 in the cyanobacterium Synechococcus sp. PCC 7942.

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