<i>Arabidopsis</i>Protein Disulfide Isomerase-5 Inhibits Cysteine Proteases during Trafficking to Vacuoles before Programmed Cell Death of the Endothelium in Developing Seeds

Ondzighi, Christine Andème; Christopher, David A.; Cho, Eun Ju; Chang, Shu-Choeng; Staehelin, L. Andrew

doi:10.1105/tpc.108.058339

Cited by 151 publications

(87 citation statements)

References 97 publications

(111 reference statements)

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“…However, little is known about their functions and their subcellular locations in Arabidopsis seeds. It has been reported that PDI5 (At1g21750) chaperones and inhibits cysteine proteases during trafficking to vacuoles prior to programmed cell death of the endothelium in developing seeds (86), and this protein is oxidized during Arabidopsis seed germination (50). In rice seeds, a PDI protein (LOC_Os11g09280) prevents proglutelin and prolamin from aggregating by chaperoning their segregation in the ER lumen (87,88).…”

Section: Discussionmentioning

confidence: 99%

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Dynamic Proteomics Emphasizes the Importance of Selective mRNA Translation and Protein Turnover during Arabidopsis Seed Germination

Galland¹,

Huguet²,

Arc³

et al. 2014

Molecular & Cellular Proteomics

142

155

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During seed germination, the transition from a quiescent metabolic state in a dry mature seed to a proliferative metabolic state in a vigorous seedling is crucial for plant propagation as well as for optimizing crop yield. This work provides a detailed description of the dynamics of protein synthesis during the time course of germination, demonstrating that mRNA translation is both sequential and selective during this process. The complete inhibition of the germination process in the presence of the translation inhibitor cycloheximide established that mRNA translation is critical for Arabidopsis seed germination. However, the dynamics of protein turnover and the selectivity of protein synthesis (mRNA translation) during Arabidopsis seed germination have not been addressed yet. Based on our detailed knowledge of the Arabidopsis seed proteome, we have deepened our understanding of seed mRNA translation during germination by combining twodimensional gel-based proteomics with dynamic radiolabeled proteomics using a radiolabeled amino acid precursor, namely [35 S]-methionine, in order to highlight de novo protein synthesis, stability, and turnover. Our data confirm that during early imbibition, the Arabidopsis translatome keeps reflecting an embryonic maturation program until a certain developmental checkpoint. Furthermore, by dividing the seed germination time lapse into discrete time windows, we highlight precise and specific patterns of protein synthesis. These data refine and deepen our knowledge of the three classical phases of seed germination based on seed water uptake during imbibition and reveal that selective mRNA translation is a key feature of seed germination. Beyond the quantitative control of translational activity, both the selectivity of mRNA translation and protein turnover appear as specific regulatory systems, critical for timing the molecular events leading to successful germination and seedling establishment. Molecular & Cellular Proteomics 13: 10.1074/mcp.M113.032227, 252-268, 2014.Seed germination is a vital stage in the plant life cycle during which embryo cells experience a programmed transition from a quiescent to a highly active metabolic state. Accordingly, seed quality in terms of germination vigor is of paramount importance for both ecological aspects and practical applications, as it influences the level, timing, and uniformity of seedling emergence in a wide range of environmental conditions (1, 2). In efforts to decipher the complex molecular mechanisms that control seed germination, genetic, genomic, and postgenomic analyses have been developed on the model plant Arabidopsis thaliana (3-6). Germination is classically described as a sequential time course divided into three major phases of seed water uptake (7). Phase I is characterized by rapid seed imbibition, which is crucial for the transition from the quiescent metabolic state of the dry seed to the high metabolic activity of the hydrated seed. Phase II corresponds to a period during which the seed imbibition level remains const...

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Section: Discussionmentioning

confidence: 99%

“…The Arabidopsis genome contains 12 PDI genes (86). PDIs are thiodisulfide oxidoreductases that catalyze disulfide bond formation and rearrangements in the substrate proteins, facilitating the folding of nascent polypeptides in the endoplasmic reticulum (ER).…”

Section: Discussionmentioning

confidence: 99%

Dynamic Proteomics Emphasizes the Importance of Selective mRNA Translation and Protein Turnover during Arabidopsis Seed Germination

Galland¹,

Huguet²,

Arc³

et al. 2014

Molecular & Cellular Proteomics

142

155

View full text Add to dashboard Cite

show abstract

“…In the soybean (Glycine max) cotyledon, P5 subfamily oxidoreductase PDIM associates noncovalently with proglycinin, 11S globulin-type storage protein (Wadahama et al, 2008). In Arabidopsis, PDI5 (PDIL1;1) regulates the timing of programmed cell death in endothelial cells (Andè me Ondzighi et al, 2008), and PDIL2;1 plays a role in embryo sac development (Wang et al, 2008). In Arabidopsis liquid culture, the PDI family oxidoreductases respond differently to various types of stresses (Lu and Christopher, 2008).…”

Section: Introductionmentioning

confidence: 99%

Distinct Roles of Protein Disulfide Isomerase and P5 Sulfhydryl Oxidoreductases in Multiple Pathways for Oxidation of Structurally Diverse Storage Proteins in Rice

et al. 2011

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In the rice (Oryza sativa) endosperm, storage proteins are synthesized on the rough endoplasmic reticulum (ER), in which prolamins are sorted to protein bodies (PBs) called type-I PB (PB-I). Protein disulfide isomerase (PDI) family oxidoreductase PDIL2;3, an ortholog of human P5, contains a conserved structural disulfide in the redox-inactive thioredoxin-like (TRX) domain and was efficiently targeted to the surface of PB-I in a redox active site-dependent manner, whereas PDIL1;1, an ortholog of human PDI, was localized in the ER lumen. Complementation analyses using PDIL1;1 knockout esp2 mutant indicated that the a and a9 TRX domains of PDIL1;1 exhibited similar redox activities and that PDIL2;3 was unable to perform the PDIL1;1 functions. PDIL2;3 knockdown inhibited the accumulation of Cys-rich 10-kD prolamin (crP10) in the core of PB-I. Conversely, crP10 knockdown dispersed PDIL2;3 into the ER lumen. Glutathione S-transferase-PDIL2;3 formed a stable tetramer when it was expressed in Escherichia coli, and the recombinant PDIL2;3 tetramer facilitated a-globulin(C79F) mutant protein to form nonnative intermolecular disulfide bonds in vitro. These results indicate that PDIL2;3 and PDIL1;1 are not functionally redundant in sulfhydryl oxidations of structurally diverse storage proteins and play distinct roles in PB development. We discuss PDIL2;3-dependent and PDIL2;3-independent oxidation pathways that sustain disulfide bonds of crP10 in PB-I.

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“…Chaperoning and inhibition of cysteine proteases by protein disulfide isomerase-5 during trafficking to vacuole before PCD [56] Vacuole (PSV and Lytic Vacuole)…”

Section: Er-derived Compartments Accumulation and Release Of Cysteinementioning

confidence: 99%

A comparison between nuclear dismantling during plant and animal programmed cell death

Domı́nguez

Cejudo

2012

Plant Science

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Programmed cell death (PCD) is a process of organized destruction of cells, essential for the development and maintenance of cellular homeostasis of multicellular organisms. Cells undergoing PCD begin a degenerative process in response to internal or external signals, whereby the nucleus becomes one of the targets. The process of nuclear dismantling includes events affecting the nuclear envelope, such as formation of lobes at the nuclear surface, selective proteolysis of nucleoporins and nuclear pore complex clustering. In addition, chromatin condensation increases in coordination with DNA fragmentation. These processes have been largely studied in animals, but remain poorly understood in plants. The overall process of cell death has different morphological and biochemical features in plants and animals. However, recent advances suggest that nuclear dismantling in plant cells progresses with morphological and biochemical characteristics similar to those in apoptotic animal cells. In this review, we summarize nuclear dismantling in plant PCD, focusing on the similarities and differences with their animal counterparts.

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ArabidopsisProtein Disulfide Isomerase-5 Inhibits Cysteine Proteases during Trafficking to Vacuoles before Programmed Cell Death of the Endothelium in Developing Seeds

Cited by 151 publications

References 97 publications

Dynamic Proteomics Emphasizes the Importance of Selective mRNA Translation and Protein Turnover during Arabidopsis Seed Germination

Dynamic Proteomics Emphasizes the Importance of Selective mRNA Translation and Protein Turnover during Arabidopsis Seed Germination

Distinct Roles of Protein Disulfide Isomerase and P5 Sulfhydryl Oxidoreductases in Multiple Pathways for Oxidation of Structurally Diverse Storage Proteins in Rice

A comparison between nuclear dismantling during plant and animal programmed cell death

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