No plastidial calmodulin-like proteins detected by two targeted mass-spectrometry approaches and GFP fusion proteins

Dell’Aglio, Elisa; Salvi, Daniel; Kraut, Alexandra; Baudet, Mathieu; Macherel, David; Neveu, Martine; Ferro, Myriam; Curien, Gilles; Rolland, Norbert

doi:10.1016/j.neps.2016.08.001

Cited by 5 publications

(4 citation statements)

References 73 publications

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“…1c), indicating its ability to bind Ca 2+ . This result is consistent with the recent report that CML41 binds to phenyl sepharose in a Ca 2+ -dependent manner (Dell'Aglio et al, 2016).…”

Section: Resultssupporting

confidence: 94%

A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses

Cheval

Laohavisit

et al. 2017

New Phytologist

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Summary Plants sense microbial signatures via activation of pattern recognition receptors (PPRs), which trigger a range of cellular defences. One response is the closure of plasmodesmata, which reduces symplastic connectivity and the capacity for direct molecular exchange between host cells.Plasmodesmal flux is regulated by a variety of environmental cues but the downstream signalling pathways are poorly defined, especially the way in which calcium regulates plasmodesmal closure.Here, we identify that closure of plasmodesmata in response to bacterial flagellin, but not fungal chitin, is mediated by a plasmodesmal‐localized Ca2+‐binding protein Calmodulin‐like 41 (CML41). CML41 is transcriptionally upregulated by flg22 and facilitates rapid callose deposition at plasmodesmata following flg22 treatment. CML41 acts independently of other defence responses triggered by flg22 perception and reduces bacterial infection.We propose that CML41 enables Ca2+‐signalling specificity during bacterial pathogen attack and is required for a complete defence response against Pseudomonas syringae.

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“…1c), indicating its ability to bind Ca 2+ . This result is consistent with the recent report that CML41 binds to phenyl sepharose in a Ca 2+ -dependent manner (Dell'Aglio et al, 2016).…”

Section: Resultssupporting

confidence: 94%

A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses

Cheval

Laohavisit

et al. 2017

New Phytologist

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“…For decades, the Ca 2+ /Calmodulin (CaM)-dependence of NADK activity has been recognized (Muto and Miyachi, 1977; Anderson et al, 1980; Karita et al, 2004) and NADK2 was reported capable of binding to CaM in vitro (Turner et al, 2004). However, no candidate CaM and no response to Ca 2+ in NADK2 activity have been reported elsewhere (Dell’Aglio et al, 2016). Instead of NADK2, it was recently reported that Arabidopsis P-loop ATPase has CaM-dependent NADK activity (Dell’Aglio et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Inter-Organelle NAD Metabolism Underpinning Light Responsive NADP Dynamics in Plants

Hashida

Kawai‐Yamada

2019

Front. Plant Sci.

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Upon illumination, photosystem I in chloroplasts catalyzes light-driven electron transport from plastocyanin to ferredoxin, followed by the reduction of NADP + to NADPH by ferredoxin:NADP + reductase for CO 2 fixation. At the beginning of photosynthesis, NADP + supply control is dominated by de novo NADP + synthesis rather than being recycled from the Calvin cycle. Importantly, ferredoxin distributes electrons to NADP + as well as to thioredoxins for light-dependent regulatory mechanisms, to cyclic electron flow for more adenosine triphosphate (ATP) production, and to several metabolites for reductive reactions. We previously demonstrated that the NADP + synthesis activity and the amount of the NADP pool size, namely the sum of NADP + and NADPH, varies depending on the light conditions and the ferredoxin-thioredoxin system. In addition, the regulatory mechanism of cytoplasmic NAD + supply is also involved in the chloroplastic NADP + supply control because NAD + is an essential precursor for NADP + synthesis. In this mini-review, we summarize the most recent advances on our understanding of the regulatory mechanisms of NADP + production, focusing on the interactions, crosstalk, and co-regulation between chloroplasts and the cytoplasm at the level of NAD + metabolism and molecular transport.

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“…For decades, it has been proposed that a large amount of plant NADK is strictly dependent on the presence of Ca 2+ and calmodulin (CaM) (Muto and Miyachi, 1977;Anderson et al, 1980;Karita et al, 2004). Even now, the Ca 2+ /CaM-dependence of NADK regulation is still controversial because of several discrepancies between in vitro assays and subcellular localizations of NADK and CaM (Turner et al, 2004;Dell'Aglio et al, 2016). Besides its dependence on CaM, NADK activity may be regulated by its reduction state and phytochrome levels (Tezuka and Yamamoto, 1975;Delumeau et al, 2000), although there have been unfortunately no further reports on these subjects to date.…”

Section: Introductionmentioning

confidence: 99%

Ferredoxin/thioredoxin system plays an important role in the chloroplastic NADP status of Arabidopsis

et al. 2018

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NADP is a key electron carrier for a broad spectrum of redox reactions, including photosynthesis. Hence, chloroplastic NADP status, as represented by redox status (ratio of NADPH to NADP ) and pool size (sum of NADPH and NADP ), is critical for homeostasis in photosynthetic cells. However, the mechanisms and molecules that regulate NADP status in chloroplasts remain largely unknown. We have now characterized an Arabidopsis mutant with imbalanced NADP status (inap1), which exhibits a high NADPH/NADP ratio and large NADP pool size. inap1 is a point mutation in At2g04700, which encodes the catalytic subunit of ferredoxin/thioredoxin reductase. Upon illumination, inap1 demonstrated earlier increases in NADP pool size than the wild type did. The mutated enzyme was also found in vitro to inefficiently reduce m-type thioredoxin, which activates Calvin cycle enzymes, and NADP-dependent malate dehydrogenase to export reducing power to the cytosol. Accordingly, Calvin cycle metabolites and amino acids diminished in inap1 plants. In addition, inap1 plants barely activate NADP-malate dehydrogenase, and have an altered redox balance between the chloroplast and cytosol, resulting in inefficient nitrate reduction. Finally, mutants deficient in m-type thioredoxin exhibited similar light-dependent NADP dynamics as inap1. Collectively, the data suggest that defects in ferredoxin/thioredoxin reductase and m-type thioredoxin decrease the consumption of NADPH, leading to a high NADPH/NADP ratio and large NADP pool size. The data also suggest that the fate of NADPH is an important influence on NADP pool size.

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No plastidial calmodulin-like proteins detected by two targeted mass-spectrometry approaches and GFP fusion proteins

Abstract: Supplementary data: http://dx.doi.org/10.1016/j.neps.2016.08.001International audienc

Cited by 5 publications

References 73 publications

A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses

A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses

Inter-Organelle NAD Metabolism Underpinning Light Responsive NADP Dynamics in Plants

Ferredoxin/thioredoxin system plays an important role in the chloroplastic NADP status of Arabidopsis

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