Glycosylation of phytepsin and expression of dad1 , dad2 and ost1 during onset of cell death in germinating barley scutella

Lindholm, Päivi; Kuittinen, T.; Sorri, Outi; Guo, Deyin; Merits, Andres; Törmäkangas, Kirsi; Runeberg-Roos, Pia

doi:10.1016/s0925-4773(00)00254-9

Cited by 37 publications

(26 citation statements)

References 24 publications

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“…Northern blot analysis of germinating barley scutella show that the expression of only dad1 declined before the onset of DNA fragmentation. In contrast to this, the expression of another dad transcript dad2 and ost1 (a cDNA encoding another subunit of the same OST complex) increases before the onset of DNA fragmentation (Lindholm et al 2000). On the other hand, the plant homologue of the dad gene is downregulated during senescence of fl ower petals in pea (Orzaez and Granell 1997).…”

Section: Discussionmentioning

confidence: 99%

A homologue of the defender against the apoptotic death gene (dad1) in UV-exposed Chlamydomonas cells is downregulated with the onset of programmed cell death

2007

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We report here the isolation of a homologue of the potential anti-apoptotic gene, defender against apoptotic death (dad1 )from Chlamydomonas reinhardtii cells.Using polymerase chain reaction (PCR),we investigated its expression in the execution process of programmed cell death (PCD)in UV-C exposed dying C.reinhardtii cells.Reverse- transcriptase (RT)-PCR showed that C.reinhardtii dad1 amplification was drastically reduced in UV-C exposed dying C.reinhardtii cells.We connect the downregulation of dad1 with the upregulation of apoptosis protease activating factor-1 (APAF-1)and the physiological changes that occur in C.reinhardtii cells upon exposure to 12 J/m 2 UV-C in order to show a reciprocal relationship between proapoptotic and inhibitor of apoptosis factors.The temporal changes indicate a correlation between the onset of cell death and dad1 downregulation.The sequence of the PCR product of the cDNA encoding the dad1 homologue was aligned with the annotated dad1 (C_20215)from the Chlamydomonas database (http://genome.jgi-psf.org:8080/annotator/servlet/jgi.annotation.Annotation?pDb=chlre2); Annotation?pDb=chlre2 );this sequence was found to show 100% identity,both at the nucleotide and amino acid level. The 327 bp transcript showed an open reading frame of 87 amino acid residues.The deduced amino acid sequence of the putative C.reinhardtii DAD1 homologue showed 54% identity with Oryza sativa, 56 identity with Drosophila melanogaster, 66% identity with Xenopus laevis, and 64% identity with Homo sapiens,Sus scrofa,Gallus gallus,Rattus norvegicus and Mus musculus.

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Section: Discussionmentioning

confidence: 99%

A homologue of the defender against the apoptotic death gene (dad1) in UV-exposed Chlamydomonas cells is downregulated with the onset of programmed cell death

2007

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“…Plant aspartic proteases have been implicated in a variety of physiological processes where cell death events play a key role (7,(22)(23)(24)(25). Activation of these proteases therefore triggers the onset of these events and determines the fate of the plant cell.…”

Section: Discussionmentioning

confidence: 99%

Activation, Proteolytic Processing, and Peptide Specificity of Recombinant Cardosin A

Castanheira

Samyn

Sergeant

et al. 2005

Journal of Biological Chemistry

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Cardosins are model plant aspartic proteases, a group of proteases that are involved in cell death events associated with plant senescence and stress responses. They are synthesized as single-chain zymogens, and subsequent conversion into two-chain mature enzymes is a crucial step in the regulation of their activity. Here we describe the activation and proteolytic processing of recombinant procardosin A. The cleavage sites involved in this multi-step autocatalytic process were determined, some of them using a novel method for C-terminal sequence analysis. Even though the two-chain recombinant enzyme displayed similar properties as natural cardosin A, a single-chain mutant form was engineered based on the processing results and produced in Escherichia coli. Determination of its primary specificity using two combinatorial peptide libraries revealed that this mutant form behaved like the natural enzyme. The primary specificity of the enzyme closely resembles those of cathepsin D and plasmepsins, suggesting that cardosin A shares the same peptide scissile bond preferences of its vacuolar/lysosomal mammalian and protozoan homologues.Sequencing of the Arabidopsis genome unveiled over 50 genes coding for aspartic proteases of the pepsin type (1, 2). These genes have been assigned to three different categories: typical, nucellin-like, and atypical proteases (2). With the exception of the products of cnd41 (3-5) and cdr1 (6) genes, very little is known about the nucellin and the atypical subgroups. In fact, most of the knowledge acquired during the last decade relates to the typical subgroup of plant aspartic proteases and has been generated predominantly from the study of phytepsin from barley seeds and cardosins from the flowers of cardoon (7).Typical plant aspartic proteases constitute a set of enzymes that share many structural and functional features not only among them but also with some of their mammalian and microbial homologues. They display activity at acidic pH and are inhibited by pepstatin A, a natural hexapeptide from Streptomyces. Common features also include the overall three-dimensional structure of mature enzymes, the catalytic apparatus, and a conserved DT/SG motif. A distinguishing feature of typical plant aspartic proteases is the occurrence of an extra 100-amino acid-long internal segment, known as the plant-specific insert (PSI), in the sequence of their precursors. This domain displays structural and functional similarities to saposins (8, 9), sphingolipid-activating proteins from animals, and some antimicrobial peptides such as NK-lysin, granulysin, and amoebapores (10); it folds as an independent domain in the precursor form (11) and is subsequently excised to generate the mature two-chain form (7). Even though the function of PSI 1 is not yet fully elucidated, it seems to play an important role in targeting plant aspartic protease precursors to the vacuole (11,12).Little is known regarding the function of typical plant aspartic proteases. Colocalization studies with putative substrates and thei...

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“…7b). DAD-1 encodes a subunit of oligosaccharyltransferase, which participates in N-linked protein glycosylation in the ER, a post-transcriptional modification fundamental for proper protein folding (Lindholm et al 2000;review by Schröder and Kaufman 2005). Inhibition of N-linked protein glycosylation results in accumulation of unfolded proteins in the ER lumen, initiating the UPR, which, in turn, triggers PCD (reviews by Urade 2009; Cacas 2010).…”

Section: W-pcd Seems To Be Induced By Er Stress-uprmentioning

confidence: 99%

The fatal effect of tungsten on Pisum sativum L. root cells: indications for endoplasmic reticulum stress-induced programmed cell death

Adamakis

Panteris

Eleftheriou

2011

Planta

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Programmed cell death (PCD) is a widespread response of plants against abiotic stress, such as heavy metal toxicity. Tungsten (W) is increasingly considered toxic for plants since it irreversibly affects their growth. Therefore, we investigated whether W could induce some kind of PCD in plants, like other heavy metals do. The morphology of cell and nucleus, the integrity of the cytoskeleton, Evans Blue absorbance and the expression of PCD-related genes were used as indicators of PCD in W-treated roots of Pisum sativum (pea). TEM and fluorescence microscopy revealed mitotic cycle arrest, protoplast shrinkage, disruption of the cytoskeleton and chromatin condensation and peripheral distribution in the nucleus of W-affected cells. Moreover, Evans Blue absorbance in roots increased in relation to the duration of W treatment. These effects were suppressed by inhibitors of the 26S proteasome, caspases and endoplasmic reticulum stress. In addition, silencing of DAD-1 and induction of HSR203J, BiP-D, bZIP28 and bZIP60 genes were also recorded in W-treated pea roots by semi-quantitative RT-PCR. The above observations show that W induces a kind of PCD in pea roots, further substantiating its toxicity for plants. Data imply that endoplasmic reticulum stress-unfolded protein response may be involved in W-induced PCD.

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Glycosylation of phytepsin and expression of dad1 , dad2 and ost1 during onset of cell death in germinating barley scutella

Cited by 37 publications

References 24 publications

A homologue of the defender against the apoptotic death gene (dad1) in UV-exposed Chlamydomonas cells is downregulated with the onset of programmed cell death

A homologue of the defender against the apoptotic death gene (dad1) in UV-exposed Chlamydomonas cells is downregulated with the onset of programmed cell death

Activation, Proteolytic Processing, and Peptide Specificity of Recombinant Cardosin A

The fatal effect of tungsten on Pisum sativum L. root cells: indications for endoplasmic reticulum stress-induced programmed cell death

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