Small Cab-like Proteins Retard Degradation of Photosystem II-associated Chlorophyll in Synechocystis sp. PCC 6803

Vavilin, Dmitrii V.; Yao, Danny; Vermaas, Wim F. J.

doi:10.1074/jbc.m707133200

Cited by 61 publications

(42 citation statements)

References 41 publications

(99 reference statements)

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“…In addition, Small Cab-like Proteins (SCPs), single transmembrane helix proteins with similarity to part of chlorophyll a/b-binding light harvesting proteins in plants, have been shown to be involved in PSII chlorophyll recycling [15,17]. There is also evidence that SCPs stabilize PSI complexes [18].…”

Section: Introductionmentioning

confidence: 99%

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

2011

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Edited by Richard CogdellKeywords: Photosystem I Photosystem II Small Cab-like protein Protein turnover Half-life time a b s t r a c tThe half-life times of photosystem I and II proteins were determined using 15 N-labeling and mass spectrometry. The half-life times (30-75 h for photosystem I components and <1-11 h for the large photosystem II proteins) were similar when proteins were isolated from monomeric vs. oligomeric complexes on Blue-Native gels, suggesting that the two forms of both photosystems can interchange on a timescale of <1 h or that only one form of each photosystem exists in thylakoids in vivo. The half-life times of proteins associated with either photosystem generally were unaffected by the absence of Small Cab-like proteins.

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Section: Introductionmentioning

confidence: 99%

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

2011

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“…7). Recent results showing the association of so-called high light-induced proteins with PSII (Promnares et al, 2006;Yao et al, 2007) and their presumable role in the temporary binding of Chl during the PSII repair-related D1 replacement (Vavilin et al, 2007) indicate that Chl molecules released from the degraded D1 can be reused. It is possible that the lack of the newly synthesized CP47 allows more Chl precursors to be utilized for the synthesis of Chl consumed during selective D1 turnover.…”

Section: Role Of Psb28 Protein In the Synthesis Of Chl And Chl-bindinmentioning

confidence: 99%

Psb28 Protein Is Involved in the Biogenesis of the Photosystem II Inner Antenna CP47 (PsbB) in the Cyanobacterium Synechocystis sp. PCC 6803

et al. 2008

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The role of the Psb28 protein in the structure and function of the photosystem II (PSII) complex has been studied in the cyanobacterium Synechocystis sp. PCC 6803. The protein was localized in the membrane fraction and, whereas most of the protein was detected as an unassembled protein, a small portion was found in the PSII core complex lacking the CP43 antenna (RC47). The association of Psb28 with RC47 was further confirmed by preferential isolation of RC47 from the strain containing a histidine-tagged derivative of Psb28 using nickel-affinity chromatography. However, the affinity-purified fraction also contained a small amount of the unassembled PSII inner antenna CP47 bound to Psb28-histidine, indicating a structural relationship between Psb28 and CP47. A psb28 deletion mutant exhibited slower autotrophic growth than wild type, although the absence of Psb28 did not affect the functional properties of PSII. The mutant showed accelerated turnover of the D1 protein, faster PSII repair, and a decrease in the cellular content of PSI. Radioactive labeling revealed a limitation in the synthesis of both CP47 and the PSI subunits PsaA/PsaB in the absence of Psb28. The mutant cells contained a high level of magnesium protoporphyrin IX methylester, a decreased level of protochlorophyllide, and released large quantities of protoporphyrin IX into the medium, indicating inhibition of chlorophyll (Chl) biosynthesis at the cyclization step yielding the isocyclic ring E. Overall, our results show the importance of Psb28 for synthesis of Chls and/or apoproteins of Chl-binding proteins CP47 and PsaA/PsaB.

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“…The genes differentially regulated by oxidative stress also include the high-light-inducible proteins encoding genes, three of which are induced at higher levels in HL cells than in LL cells (hli_0937, hli_0797, hli_1441). HL-inducible proteins have been shown to be involved in protecting cells against photodamage, either by direct or indirect dissipation of excess absorbed light energy (Montané and Kloppstech, 2000;He et al, 2001;Havaux et al, 2003) or by binding and storage of free chlorophylls (Funk and Vermaas, 1999;Vavilin et al, 2007;Kufryk et al, 2008).…”

Section: Transcriptome Response To Oxidative Stressmentioning

confidence: 99%

Light History Influences the Response of the Marine CyanobacteriumSynechococcussp. WH7803 to Oxidative Stress

et al. 2011

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Marine Synechococcus undergo a wide range of environmental stressors, especially high and variable irradiance, which may induce oxidative stress through the generation of reactive oxygen species (ROS). While light and ROS could act synergistically on the impairment of photosynthesis, inducing photodamage and inhibiting photosystem II repair, acclimation to high irradiance is also thought to confer resistance to other stressors. To identify the respective roles of light and ROS in the photoinhibition process and detect a possible light-driven tolerance to oxidative stress, we compared the photophysiological and transcriptomic responses of Synechococcus sp. WH7803 acclimated to low light (LL) or high light (HL) to oxidative stress, induced by hydrogen peroxide (H 2 O 2 ) or methylviologen. While photosynthetic activity was much more affected in HL than in LL cells, only HL cells were able to recover growth and photosynthesis after the addition of 25 mM H 2 O 2 . Depending upon light conditions and H 2 O 2 concentration, the latter oxidizing agent induced photosystem II inactivation through both direct damage to the reaction centers and inhibition of its repair cycle. Although the global transcriptome response appeared similar in LL and HL cells, some processes were specifically induced in HL cells that seemingly helped them withstand oxidative stress, including enhancement of photoprotection and ROS detoxification, repair of ROS-driven damage, and regulation of redox state. Detection of putative LexA binding sites allowed the identification of the putative LexA regulon, which was downregulated in HL compared with LL cells but up-regulated by oxidative stress under both growth irradiances.

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Small Cab-like Proteins Retard Degradation of Photosystem II-associated Chlorophyll in Synechocystis sp. PCC 6803

Cited by 61 publications

References 41 publications

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

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

Psb28 Protein Is Involved in the Biogenesis of the Photosystem II Inner Antenna CP47 (PsbB) in the Cyanobacterium Synechocystis sp. PCC 6803

Light History Influences the Response of the Marine CyanobacteriumSynechococcussp. WH7803 to Oxidative Stress

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