Ssr2998 of Synechocystis sp. PCC 6803 Is Involved in Regulation of Cyanobacterial Electron Transport and Associated with the Cytochrome b6f Complex

Volkmer, Thomas; Schneider, Dirk; Bernát, Gábor; Kirchhoff, Helmut; Wenk, Stephan-Olav; Rögner, Matthias

doi:10.1074/jbc.m604948200

Cited by 28 publications

(16 citation statements)

References 43 publications

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“…A similar effect was recently reported for Synechocystis with the deleted ssr2998 gene (37). In these mutants the limited capabilities to control the PQ redox level by state transitions is compensated by adjusting the PS2 to PS1 ratio (37,40). The lowered PC/APC ratio in the ⌬petC1 strain (Table 1, Fig.…”

Section: Discussionsupporting

confidence: 57%

“…5 l of supernatant was separated by SDS-PAGE on a 12% SDS gel (49) and blotted on a polyvinylidene difluoride membrane. PetC1/2/3, cytochrome f, cytochrome b 6 , SU IV, as well as the CydA subunit of the cytochrome-bd oxidase were detected by immunoblotting using polyclonal antibodies (37,41). The PetC2 and CydA antibodies was raised against synthesized peptide fragments DQIFISP-WTDLDPRTGEKP (Iwaki, Tokyo, Japan) and KLAAMEAL-WETVPA (Davids Biotechnologie, Regensburg, Germany), respectively.…”

Section: Methodsmentioning

confidence: 99%

“…Except for PetL and PetM all subunits are required for a functional cytochrome b 6 f complex (34,35). Besides these bona fide subunits additional weakly associated subunits are also reported (36,37). The PetC (Rieske) protein has a single N-terminal located transmembrane helix followed by a mobile, water-soluble domain with the [2Fe-2S] cofactor binding regions, which extends into the thylakoid lumen.…”

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confidence: 99%

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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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Section: Discussionsupporting

confidence: 57%

Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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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 addition to these "consensus" subunits, further components with weaker binding affinities and/or transient interactions with the complex could be identified: In green algae and higher plants, binding of the ferredoxin-NADP reductase (FNR) (Zhang et al, 2001) and of the subunit PetO, which is possibly involved in the regulation of state transitions (Hamel et al, 2000) has been shown. Also, we recently showed the presence of a potentially new b 6 f subunit, PetP, in b 6 f-preprations from both the mesophilic cyanobacterium Synechocystis PCC 6803 and the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 (Volkmer et al, 2007;Gendrullis et al, 2008;Nowaczyk et al, 2010). Most remarkably, this protein is highly conserved in cyanobacteria and red algae, but not present in green algae and plants (Volkmer et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Functional Characterization of the Small Regulatory Subunit PetP from the Cytochrome b₆f Complex in Thermosynechococcus elongatus

Rexroth

Veit

et al. 2014

Plant Cell

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The cyanobacterial cytochrome b 6 f complex is central for the coordination of photosynthetic and respiratory electron transport and also for the balance between linear and cyclic electron transport. The development of a purification strategy for a highly active dimeric b 6 f complex from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 enabled characterization of the structural and functional role of the small subunit PetP in this complex. Moreover, the efficient transformability of this strain allowed the generation of a DpetP mutant. Analysis on the whole-cell level by growth curves, photosystem II light saturation curves, and P700 + reduction kinetics indicate a strong decrease in the linear electron transport in the mutant strain versus the wild type, while the cyclic electron transport via photosystem I and cytochrome b 6 f is largely unaffected. This reduction in linear electron transport is accompanied by a strongly decreased stability and activity of the isolated DpetP complex in comparison with the dimeric wild-type complex, which binds two PetP subunits. The distinct behavior of linear and cyclic electron transport may suggest the presence of two distinguishable pools of cytochrome b 6 f complexes with different functions that might be correlated with supercomplex formation.

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“…In higher plants, cyt b 6 f has been co-isolated with FNR [86], and the functional coupling of a small phosphoprotein PetO to cyt b 6 f has been reported [87]. PetP has been proposed as a new cyanobacterial cyt b 6 f subunit that might be analogous to PetO [88].…”

Section: Regulatory Factors For Psi Assemblymentioning

confidence: 99%

Regulatory factors for the assembly of thylakoid membrane protein complexes

Chi

Zhang

2012

Phil. Trans. R. Soc. B

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Major multi-protein photosynthetic complexes, located in thylakoid membranes, are responsible for the capture of light and its conversion into chemical energy in oxygenic photosynthetic organisms. Although the structures and functions of these photosynthetic complexes have been explored, the molecular mechanisms underlying their assembly remain elusive. In this review, we summarize current knowledge of the regulatory components involved in the assembly of thylakoid membrane protein complexes in photosynthetic organisms. Many of the known regulatory factors are conserved between prokaryotes and eukaryotes, whereas others appear to be newly evolved or to have expanded predominantly in eukaryotes. Their specific features and fundamental differences in cyanobacteria, green algae and land plants are discussed.

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Ssr2998 of Synechocystis sp. PCC 6803 Is Involved in Regulation of Cyanobacterial Electron Transport and Associated with the Cytochrome b6f Complex

Cited by 28 publications

References 43 publications

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

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

Functional Characterization of the Small Regulatory Subunit PetP from the Cytochrome b₆f Complex in Thermosynechococcus elongatus

Regulatory factors for the assembly of thylakoid membrane protein complexes

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Ssr2998 of Synechocystis sp. PCC 6803 Is Involved in Regulation of Cyanobacterial Electron Transport and Associated with the Cytochrome b6f Complex

Cited by 28 publications

References 43 publications

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

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

Functional Characterization of the Small Regulatory Subunit PetP from the Cytochrome b6f Complex in Thermosynechococcus elongatus

Regulatory factors for the assembly of thylakoid membrane protein complexes

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Functional Characterization of the Small Regulatory Subunit PetP from the Cytochrome b₆f Complex in Thermosynechococcus elongatus