The ‘protein complex proteome’ of chloroplasts in Arabidopsis thaliana

Behrens, Christof; Blume, Christian; Senkler, Jennifer; Eubel, Holger; Peterhänsel, Christoph; Braun, Hans‐Peter

doi:10.1016/j.jprot.2013.07.001

Cited by 24 publications

(13 citation statements)

References 62 publications

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“…However, only three have been confirmed so far: AtCPK20, AtCPK31, and AtCAS. It is worth to mention that CPK20, besides the plastidial localization that was confirmed by MS/MS approaches (Behrens et al, 2013), showed a plasma membrane localization when fused to reporter genes or coexpressed with other CPK members (Gutermuth et al, 2013). CPK31 has also been shown to localize at the plasma membrane when interacting with the arsenite transporter NIP1;1 (Ji et al, 2017).…”

Section: Current Knowledge Of the Molecular Players Involved In Ca 2+mentioning

confidence: 73%

Chloroplast Calcium Signaling in the Spotlight

et al. 2020

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Calcium has long been known to regulate the metabolism of chloroplasts, concerning both light and carbon reactions of photosynthesis, as well as additional non photosynthesis-related processes. In addition to undergo Ca 2+ regulation, chloroplasts can also influence the overall Ca 2+ signaling pathways of the plant cell. Compelling evidence indicate that chloroplasts can generate specific stromal Ca 2+ signals and contribute to the fine tuning of cytoplasmic Ca 2+ signaling in response to different environmental stimuli. The recent set up of a toolkit of genetically encoded Ca 2+ indicators, targeted to different chloroplast subcompartments (envelope, stroma, thylakoids) has helped to unravel the participation of chloroplasts in intracellular Ca 2+ handling in resting conditions and during signal transduction. Intra-chloroplast Ca 2+ signals have been demonstrated to occur in response to specific environmental stimuli, suggesting a role for these plant-unique organelles in transducing Ca 2+ -mediated stress signals. In this mini-review we present current knowledge of stimulus-specific intrachloroplast Ca 2+ transients, as well as recent advances in the identification and characterization of Ca 2+ -permeable channels/transporters localized at chloroplast membranes. In particular, the potential role played by cMCU, a chloroplast-localized member of the mitochondrial calcium uniporter (MCU) family, as component of plant environmental sensing is discussed in detail, taking into account some specific structural features of cMCU. In summary, the recent molecular identification of some players of chloroplast Ca 2+ signaling has opened new avenues in this rapidly developing field and will hopefully allow a deeper understanding of the role of chloroplasts in shaping physiological responses in plants.

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Section: Current Knowledge Of the Molecular Players Involved In Ca 2+mentioning

confidence: 73%

Chloroplast Calcium Signaling in the Spotlight

et al. 2020

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“…This was supported by a previous proteome analysis using chloroplasts isolated from Arabidopsis leaves. 42,43) In order to confirm this in more detail, cDNA was cloned into the pGWB505 vector for the expression of DHAR3-cGFP fusion proteins. When the fusion proteins were transiently expressed in the leaves of 4-week-old wild-type Arabidopsis plants, GFP fluorescence clearly overlapped with the red fluorescence derived from chloroplasts (Fig.…”

Section: Resultsmentioning

confidence: 99%

Redox regulation of ascorbate and glutathione by a chloroplastic dehydroascorbate reductase is required for high-light stress tolerance in Arabidopsis

Noshi

Hatanaka

Tanabe

et al. 2016

Bioscience, Biotechnology, and Biochemistry

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Chloroplasts are a significant site for reactive oxygen species production under illumination and, thus, possess a well-organized antioxidant system involving ascorbate. Ascorbate recycling occurs in different manners in this system, including a dehydroascorbate reductase (DHAR) reaction. We herein investigated the physiological significance of DHAR3 in photo-oxidative stress tolerance in Arabidopsis. GFP-fused DHAR3 protein was targeted to chloroplasts in Arabidopsis leaves. A DHAR3 knockout mutant exhibited sensitivity to high light (HL). Under HL, the ascorbate redox states were similar in mutant and wild-type plants, while total ascorbate content was significantly lower in the mutant, suggesting that DHAR3 contributes, at least to some extent, to ascorbate recycling. Activation of monodehydroascorbate reductase occurred in dhar3 mutant, which might compensate for the lack of DHAR3. Interestingly, glutathione oxidation was consistently inhibited in dhar3 mutant. These findings indicate that DHAR3 regulates both ascorbate and glutathione redox states to acclimate to HL.

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“…It is most likely because chloroplasts in leaf cell are numerous and are rich in soluble proteins, such as Rubisco, Rubisco activase, and ATP synthase, which account for more than half of the total soluble proteins in mature leaf cells [43,75,76]. The bioinformatic analysis with WolfPsort revealed that nearly 82% of the identified proteins from chloroplast were predicted to be typical chloroplast proteins, indicating the high purity of chloroplast isolation.…”

Section: Discussionmentioning

confidence: 99%

Comparative Proteomic and Physiological Analysis Reveals the Variation Mechanisms of Leaf Coloration and Carbon Fixation in a Xantha Mutant of Ginkgo biloba L.

Liu

Wang

et al. 2016

IJMS

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Yellow-green leaf mutants are common in higher plants, and these non-lethal chlorophyll-deficient mutants are ideal materials for research on photosynthesis and plant development. A novel xantha mutant of Ginkgo biloba displaying yellow-colour leaves (YL) and green-colour leaves (GL) was identified in this study. The chlorophyll content of YL was remarkably lower than that in GL. The chloroplast ultrastructure revealed that YL had less dense thylakoid lamellae, a looser structure and fewer starch grains than GL. Analysis of the photosynthetic characteristics revealed that YL had decreased photosynthetic activity with significantly high nonphotochemical quenching. To explain these phenomena, we analysed the proteomic differences in leaves and chloroplasts between YL and GL of ginkgo using two-dimensional gel electrophoresis (2-DE) coupled with MALDI-TOF/TOF MS. In total, 89 differential proteins were successfully identified, 82 of which were assigned functions in nine metabolic pathways and cellular processes. Among them, proteins involved in photosynthesis, carbon fixation in photosynthetic organisms, carbohydrate/energy metabolism, amino acid metabolism, and protein metabolism were greatly enriched, indicating a good correlation between differentially accumulated proteins and physiological changes in leaves. The identifications of these differentially accumulated proteins indicates the presence of a specific different metabolic network in YL and suggests that YL possess slower chloroplast development, weaker photosynthesis, and a less abundant energy supply than GL. These studies provide insights into the mechanism of molecular regulation of leaf colour variation in YL mutants.

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The ‘protein complex proteome’ of chloroplasts in Arabidopsis thaliana

Cited by 24 publications

References 62 publications

Chloroplast Calcium Signaling in the Spotlight

Chloroplast Calcium Signaling in the Spotlight

Redox regulation of ascorbate and glutathione by a chloroplastic dehydroascorbate reductase is required for high-light stress tolerance in Arabidopsis

Comparative Proteomic and Physiological Analysis Reveals the Variation Mechanisms of Leaf Coloration and Carbon Fixation in a Xantha Mutant of Ginkgo biloba L.

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