Putative function of cytochrome b559 as a plastoquinol oxidase

Bondarava, Natallia; Groß, Christine; Mubarakshina, Maria; Golecki, Jochen R.; Johnson, Giles N.; Krieger‐Liszkay, Anja

doi:10.1111/j.1399-3054.2009.01312.x

Cited by 47 publications

(31 citation statements)

References 59 publications

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“…Moreover, in the psbO-1 mutant, Murakami et al (2002) found that the fluorescence level transiently dropped below the F 0 level during illumination, similar to what we saw in the lto1 mutant (Figure 4). This phenomenon is not limited to psbO mutants, as it was also seen recently with mutants in the cytochrome b 559 subunit of PSII (Bondarava et al, 2010). One possibility is that the PQ pool is partially reduced in the dark in the lto1 mutant and in other mutants with low PSII activity, which would result in an increased F 0 level.…”

Section: The Redox Activity Of Lto1 Is Required For the Assembly Of Psiimentioning

confidence: 74%

Lumen Thiol Oxidoreductase1, a Disulfide Bond-Forming Catalyst, Is Required for the Assembly of Photosystem II inArabidopsis

et al. 2011

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Here, we identify Arabidopsis thaliana Lumen Thiol Oxidoreductase1 (LTO1) as a disulfide bond-forming enzyme in the thylakoid lumen. Using topological reporters in bacteria, we deduced a lumenal location for the redox active domains of the protein. LTO1 can partially substitute for the proteins catalyzing disulfide bond formation in the bacterial periplasm, which is topologically equivalent to the plastid lumen. An insertional mutation within the LTO1 promoter is associated with a severe photoautotrophic growth defect. Measurements of the photosynthetic activity indicate that the lto1 mutant displays a limitation in the electron flow from photosystem II (PSII). In accordance with these measurements, we noted a severe depletion of the structural subunits of PSII but no change in the accumulation of the cytochrome b 6 f complex or photosystem I. In a yeast two-hybrid assay, the thioredoxin-like domain of LTO1 interacts with PsbO, a lumenal PSII subunit known to be disulfide bonded, and a recombinant form of the molecule can introduce a disulfide bond in PsbO in vitro. The documentation of a sulfhydryl-oxidizing activity in the thylakoid lumen further underscores the importance of catalyzed thiol-disulfide chemistry for the biogenesis of the thylakoid compartment.

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Section: The Redox Activity Of Lto1 Is Required For the Assembly Of Psiimentioning

confidence: 74%

Lumen Thiol Oxidoreductase1, a Disulfide Bond-Forming Catalyst, Is Required for the Assembly of Photosystem II inArabidopsis

et al. 2011

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“…On the contrary, cyclic electron transfer (CET) involves only one photosystem and occurs around either PSII or PSI (Shikanai, 2007;Bondarava et al, 2010;Johnson, 2011;Shinopoulos and Brudvig, 2012). Despite active research, the molecular mechanisms and biological functions of CETs are still largely unknown.…”

Section: Introductionmentioning

confidence: 99%

PROTON GRADIENT REGULATION5 Is Essential for Proper Acclimation of Arabidopsis Photosystem I to Naturally and Artificially Fluctuating Light Conditions

et al. 2012

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In nature, plants are challenged by constantly changing light conditions. To reveal the molecular mechanisms behind acclimation to sometimes drastic and frequent changes in light intensity, we grew Arabidopsis thaliana under fluctuating light conditions, in which the low light periods were repeatedly interrupted with high light peaks. Such conditions had only marginal effect on photosystem II but induced damage to photosystem I (PSI), the damage being most severe during the early developmental stages. We showed that PROTON GRADIENT REGULATION5 (PGR5)-dependent regulation of electron transfer and proton motive force is crucial for protection of PSI against photodamage, which occurred particularly during the high light phases of fluctuating light cycles. Contrary to PGR5, the NAD(P)H dehydrogenase complex, which mediates cyclic electron flow around PSI, did not contribute to acclimation of the photosynthetic apparatus, particularly PSI, to rapidly changing light intensities. Likewise, the Arabidopsis pgr5 mutant exhibited a significantly higher mortality rate compared with the wild type under outdoor field conditions. This shows not only that regulation of PSI under natural growth conditions is crucial but also the importance of PGR5 in PSI protection.

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“…Next, 1 O 2 is thought to stimulate the degradation of D1 protein (Asada and Takahashi, 1987;Krieger-Liszkay, 2005;Hideg et al, 2007;Gill and Tuteja, 2010;Vass, 2011). In addition to 1 O 2 , recent studies have revealed that superoxide (O 2 -) is also produced by PSII, which also causes photoinhibition (Bondarava et al, 2010;Zulfugarov et al, 2014). In contrast to the theory that oxidative degradation of the D1 protein causes photoinhibition in PSII, several studies now suggest that reactive oxygen species (ROS) suppress de novo D1 protein synthesis through the oxidative inactivation of the thioredoxin-regulated elongation factor G. The latter plays an important role in protein translation of the D1 protein (Kojima et al, 2007;Nishiyama et al, 2011).…”

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confidence: 99%

Superoxide and Singlet Oxygen Produced within the Thylakoid Membranes Both Cause Photosystem I Photoinhibition

et al. 2016

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Photosystem I (PSI) photoinhibition suppresses plant photosynthesis and growth. However, the mechanism underlying PSI photoinhibition has not been fully clarified. In this study, in order to investigate the mechanism of PSI photoinhibition in higher plants, we applied repetitive short-pulse (rSP) illumination, which causes PSI-specific photoinhibition in chloroplasts isolated from spinach leaves. We found that rSP treatment caused PSI photoinhibition, but not PSII photoinhibition in isolated chloroplasts in the presence of O 2 . However, chloroplastic superoxide dismutase and ascorbate peroxidase activities failed to protect PSI from its photoinhibition. Importantly, PSI photoinhibition was largely alleviated in the presence of methyl viologen, which stimulates the production of reactive oxygen species (ROS) at the stromal region by accepting electrons from PSI, even under the conditions where CuZn-superoxide dismutase and ascorbate peroxidase activities were inactivated by KCN. These results suggest that the ROS production site, but not the ROS production rate, is critical for PSI photoinhibition. Furthermore, we found that not only superoxide (O 2 2 ) but also singlet oxygen ( 1 O 2 ) is involved in PSI photoinhibition induced by rSP treatment. From these results, we suggest that PSI photoinhibition is caused by both O 2 2 and 1 O 2 produced within the thylakoid membranes when electron carriers in PSI become highly reduced. Here, we show, to our knowledge, new insight into the PSI photoinhibition in higher plants.

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Putative function of cytochrome b559 as a plastoquinol oxidase

Cited by 47 publications

References 59 publications

Lumen Thiol Oxidoreductase1, a Disulfide Bond-Forming Catalyst, Is Required for the Assembly of Photosystem II inArabidopsis

Lumen Thiol Oxidoreductase1, a Disulfide Bond-Forming Catalyst, Is Required for the Assembly of Photosystem II inArabidopsis

PROTON GRADIENT REGULATION5 Is Essential for Proper Acclimation of Arabidopsis Photosystem I to Naturally and Artificially Fluctuating Light Conditions

Superoxide and Singlet Oxygen Produced within the Thylakoid Membranes Both Cause Photosystem I Photoinhibition

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