Lifetimes of photosystem I and II proteins in the cyanobacterium <i>Synechocystis</i> sp. PCC 6803

Yao, Danny; Brune, Daniel C.; Vermaas, Wim F. J.

doi:10.1016/j.febslet.2011.12.010

Cited by 57 publications

(44 citation statements)

References 38 publications

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“…Much slower than D1 but still double the average K d of PSII and significantly different (P , , 0.001 via Dixon Q test) was PSBC, alternatively named CP43. This observation is similar to prior observations made in algae (Yao et al, 2012) and land plants (Christopher and Mullet, 1994) and is consistent with the close proximity of D1 and CP43 in the PSII structure (Kato and Sakamoto, 2009 …”

Section: Photosystemssupporting

confidence: 92%

Proteins with High Turnover Rate in Barley Leaves Estimated by Proteome Analysis Combined with in Planta Isotope Labeling

et al. 2014

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Protein turnover is a key component in cellular homeostasis; however, there is little quantitative information on degradation kinetics for individual plant proteins. We have used 15 N labeling of barley (Hordeum vulgare) plants and gas chromatography-mass spectrometry analysis of free amino acids and liquid chromatography-mass spectrometry analysis of proteins to track the enrichment of 15 N into the amino acid pools in barley leaves and then into tryptic peptides derived from newly synthesized proteins. Using information on the rate of growth of barley leaves combined with the rate of degradation of 14 N-labeled proteins, we calculate the turnover rates of 508 different proteins in barley and show that they vary by more than 100-fold. There was approximately a 9-h lag from label application until 15 N incorporation could be reliably quantified in extracted peptides. Using this information and assuming constant translation rates for proteins during the time course, we were able to quantify degradation rates for several proteins that exhibit half-lives on the order of hours. Our workflow, involving a stringent series of mass spectrometry filtering steps, demonstrates that 15 N labeling can be used for large-scale liquid chromatography-mass spectrometry studies of protein turnover in plants. We identify a series of abundant proteins in photosynthesis, photorespiration, and specific subunits of chlorophyll biosynthesis that turn over significantly more rapidly than the average protein involved in these processes. We also highlight a series of proteins that turn over as rapidly as the well-known D1 subunit of photosystem II. While these proteins need further verification for rapid degradation in vivo, they cluster in chlorophyll and thiamine biosynthesis.

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Section: Photosystemssupporting

confidence: 92%

Proteins with High Turnover Rate in Barley Leaves Estimated by Proteome Analysis Combined with in Planta Isotope Labeling

et al. 2014

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“…4). The HL sensitivity of the PSII complex to the light-induced damage necessitates a higher turnover rate of its protein subunits (especially the D1 protein) than subunits of PSI (Yao et al, 2012b). A significant disproportion between strong protein labeling versus weak Chl labeling in PSII complexes shows that the resynthesis of PSII Chl-proteins largely occurs at the expense of the recycled Chl previously released from degraded Chl-proteins.…”

Section: C]glu or [mentioning

confidence: 99%

“…On the other hand, Chl is required during the repair/replacement of PSII complexes that are photodamaged much faster than PSI complexes (Nowaczyk et al, 2006;Nixon et al, 2010). Therefore, the synthesis of Chl-binding PSII subunits, especially the fast turning over D1 subunit, should be much faster in comparison with PSI subunits (Yao et al, 2012a(Yao et al, , 2012b. It raises the question of how an enhanced synthesis of PSII subunits is achieved if less de novo-synthesized Chl is produced under HL conditions to keep PSI at a reduced level.…”

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confidence: 99%

“…However, controlling PSI content by the metabolic flow through the whole tetrapyrrole pathway does not seem to be flexible enough to balance the formation of all tetrapyrrole cofactors. The de novo Chl biosynthesis is expected to be tightly synchronized with synthesis of Chl-binding proteins (Komenda et al, 2012) but a cross talk between Chl and Chl-protein biosyntheses has to also reflect the fact that the lifetime of Chl molecules is much longer than that of proteins (Vavilin et al, 2005;Yao et al, 2012aYao et al, , 2012b; therefore, a potential role of the recycled Chl in controlling Chlprotein biogenesis must be addressed as well. In this study, we focused on the correlation between synthesis of both photosystems and Chl biosynthesis in Synechocystis cells fully acclimated to different light intensities.…”

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confidence: 99%

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Long-Term Acclimation of the Cyanobacterium Synechocystis sp. PCC 6803 to High Light Is Accompanied by an Enhanced Production of Chlorophyll That Is Preferentially Channeled to Trimeric Photosystem I

et al. 2012

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Cyanobacteria acclimate to high-light conditions by adjusting photosystem stoichiometry through a decrease of photosystem I (PSI) abundance in thylakoid membranes. As PSI complexes bind the majority of chlorophyll (Chl) in cyanobacterial cells, it is accepted that the mechanism controlling PSI level/synthesis is tightly associated with the Chl biosynthetic pathway. However, how Chl is distributed to photosystems under different light conditions remains unknown. Using radioactive labeling by 35 S and by 14 C combined with native/two-dimensional electrophoresis, we assessed the synthesis and accumulation of photosynthetic complexes in parallel with the synthesis of Chl in Synechocystis sp. PCC 6803 cells acclimated to different light intensities. Although cells acclimated to higher irradiances (150 and 300 mE m 22 s 21 ) exhibited markedly reduced PSI content when compared with cells grown at lower irradiances (10 and 40 mE m 22 s 21 ), they grew much faster and synthesized significantly more Chl, as well as both photosystems. Interestingly, even under high irradiance, almost all labeled de novo Chl was localized in the trimeric PSI, whereas only a weak Chl labeling in photosystem II (PSII) was accompanied by the intensive 35 S protein labeling, which was much stronger than in PSI. These results suggest that PSII subunits are mostly synthesized using recycled Chl molecules previously released during PSII repair-driven protein degradation. In contrast, most of the fresh Chl is utilized for synthesis of PSI complexes likely to maintain a constant level of PSI during cell proliferation.

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“…Overall, the half-life of the entire PSII complex is <11 hours, while PSI's half-life has been shown to be >30 hours. 77 Improving DET photocurrent production is also crucial because a commercial product will need to use DET rather than MET. By removing the necessity of a mediator, there is less voltage loss and possibly increased stability of the electrode.…”

Section: Future Directions and Outlookmentioning

confidence: 99%

Photobioelectrochemistry: Solar Energy Conversion and Biofuel Production with Photosynthetic Catalysts

Rasmussen

2014

J. Electrochem. Soc.

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Photobioelectrochemical cells are devices which have been developed over the past few decades and use photosynthetic catalysts for solar energy conversion or biofuel production. In this paper, a critical review of reported photobioelectrochemical systems is presented. The systems discussed include several types of photobioelectrocatalysts: whole cells, organelles, and enzymes. Special attention is paid to power or product generation as well as immobilization and electron transfer strategies used. The issues that need to be addressed in order for such systems to compete with current technologies are also discussed.

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Lifetimes of photosystem I and II proteins in the cyanobacterium Synechocystis sp. PCC 6803

Cited by 57 publications

References 38 publications

Proteins with High Turnover Rate in Barley Leaves Estimated by Proteome Analysis Combined with in Planta Isotope Labeling

Proteins with High Turnover Rate in Barley Leaves Estimated by Proteome Analysis Combined with in Planta Isotope Labeling

Long-Term Acclimation of the Cyanobacterium Synechocystis sp. PCC 6803 to High Light Is Accompanied by an Enhanced Production of Chlorophyll That Is Preferentially Channeled to Trimeric Photosystem I

Photobioelectrochemistry: Solar Energy Conversion and Biofuel Production with Photosynthetic Catalysts

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