ON SPECTRAL CONTROL OF PIGMENTATION IN ANACYSTIS NIDULANS (CYANOPHYCEAE)1,2

Myers, Jack; Graham, Jo‐Ruth; Wang, Richard T.

doi:10.1111/j.1529-8817.1978.tb02478.x

Cited by 49 publications

(36 citation statements)

References 24 publications

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“…Chromatic acclimation of photosystem stoichiometry has been widely observed in cyanobacteria, red algae, green algae, and higher plants (Myers et al, 1978(Myers et al, , 1980Manodori and Melis, 1986;Kim et al, 1993;Fujita, 1997). Namely, cells accumulate more PSI under Figure 7.…”

Section: Discussionmentioning

confidence: 99%

The Membrane-Associated CpcG2-Phycobilisome in Synechocystis: A New Photosystem I Antenna

et al. 2007

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Section: Discussionmentioning

confidence: 99%

The Membrane-Associated CpcG2-Phycobilisome in Synechocystis: A New Photosystem I Antenna

et al. 2007

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“…Phycocyanin and chlorophyll concentrations were determined according to Ref. 43, and the phycocyanin/allophycocyanin ratio as in Ref. 44.…”

Section: Methodsmentioning

confidence: 99%

Multiple Rieske Proteins Enable Short- and Long-term Light Adaptation of Synechocystis sp. PCC 6803

Tsunoyama

Bernát

Dyczmons

et al. 2009

Journal of Biological Chemistry

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In contrast to eukaryotes, most cyanobacteria contain several isoforms of the Rieske iron-sulfur protein, PetC, resulting in heterogeneity in the composition of the cytochrome b 6 f complexes. Of three isoforms in the mesophilic cyanobacterium Synechocystis PCC 6803, PetC1 is the major Rieske protein in the cytochrome b 6 f complex, whereas the physiological function of PetC2 and PetC3 is still uncertain. Comparison of wild type and various petC-deficient strains under selected light conditions revealed distinct functional differences: high-light exposure of wild type cells resulted in a significantly enhanced petC2 transcript level, whereas a ⌬petC1 mutant showed a low cytochrome b 6 f content, low electron flux, and a considerably increased accumulation of cytochrome-bd oxidase. In contrast to wild type and ⌬petC1, ⌬petC2 and ⌬petC3 strains still grew fast under high-light conditions although all three Rieske proteins are required for maximal electron transport rates. Although the presence of PetC3 appears to be required for activation of the cyclic electron transport, state transitions were more effective in the absence of PetC2 and/or PetC3. In summary, our data suggest defined roles of the various PetC proteins in short-and long-term light adaptation.

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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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ON SPECTRAL CONTROL OF PIGMENTATION IN ANACYSTIS NIDULANS (CYANOPHYCEAE)^1,²

Cited by 49 publications

References 24 publications

The Membrane-Associated CpcG2-Phycobilisome in Synechocystis: A New Photosystem I Antenna

The Membrane-Associated CpcG2-Phycobilisome in Synechocystis: A New Photosystem I Antenna

Multiple Rieske Proteins Enable Short- and Long-term Light Adaptation of Synechocystis sp. PCC 6803

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

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