Two types of aspartic proteinases from buckwheat seed – Gene structure and expression analysis

Milisavljevic, Мilan; Timotijević, Gordana; Radović, Svetlana; Konstantinović, Miroslav; Maksimović, Vesna

doi:10.1016/j.jplph.2007.03.016

Cited by 18 publications

(16 citation statements)

References 23 publications

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“…no. AAV84085), coding for the typical aspartic proteinase from buckwheat (FeAP9) (Milisavljević et al, 2008), we designed primers for isolation of the corresponding gene from genomic DNA. The complete genomic sequence of FeAP9 (acc.…”

Section: Resultsmentioning

confidence: 99%

“…In contrast to the typical aspartic proteinases, nucellin and OsAsp1 have different gene organizations containing fewer introns than typical APs (Chen and Foolad, 1997;Bi et al, 2005). In addition, a few known aspartic proteinase-like genes, such as buckwheat APL1, do not contain any introns (Milisavljević et al, 2008). Altogether, these data suggest that typical plant AP genes are derived from a common ancestor gene, and our data confirm the hypothesis that slight differences among typical APs with respect to intron arrangement and number, obviously appeared after the divergence of monocotyledonous and dicotyledonous plants, because the dicot buckwheat AP9 gene shows the highest similarity to the AP gene from the monocot rice.…”

Section: Resultsmentioning

confidence: 99%

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Ubiquitous aspartic proteinase as an actor in the stress response in buckwheat

Timotijević

Milisavljevic

Radović

et al. 2010

Journal of Plant Physiology

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Ubiquitous aspartic proteinase as an actor in the stress response in buckwheat

Timotijević

Milisavljevic

Radović

et al. 2010

Journal of Plant Physiology

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“…Phytepsins were also indirectly associated with germination in soy [44], buckwheat [43], Arabidopsis [45], wheat [41] and Araucaria [46].…”

Section: Discussionmentioning

confidence: 99%

“…In addition, two or more cDNAs for different APs were obtained from dry seeds and during germination in buckwheat [43], wheat [41], soybean [44] and Arabidopsis [45], as well as aspartyl activity was observed during seed germination in Araucaria megagametophyte [46].…”

Section: Barduche Et Al American Journal Of Plant Sciencesmentioning

confidence: 99%

Proteolysis in the Subtropical Woody Tree <i>Anadenanthera colubrina</i> (Angico) Seeds during and after Germination

Barduche¹,

Livramento²,

Júdice³

et al. 2018

AJPS

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Proteolysis of seed storage proteins (SSP) during germination provides a steady supply of amino acids to the embryo development into seedling. This process is coordinated by different peptidases that act sequentially and overlaid mode. These enzymes are an ancient group evolved separately in a wide structural and functional diversity and have many applications in medicine, pharmacy and industry. However, the knowledge about seed peptidases during germination was obtained from studies almost restricted to the cultivated species. This restriction implies caution about generalizations made from these studies, as well limits the biological knowledge about plant kingdom and technological use from plant peptidases. In this work, a scan of the proteolytic activity was held in germinating seeds of a leguminous subtropical woody tree. Eleven proteolytic activities were detected in protein extracts from embryonic axis and cotyledons. The presence and intensity of these activities varied over time and between these tissues. There was indication that aspartyl-endopeptidases (phytepsins) and cysteine-carboxypeptidases (plant cathepsins) were involved in A. colubrina SSP hydrolysis. These peptidases differ to that commonly involved in germination of the cultivated leguminous. In addition, one of detected phytepsins showed stability on pH scale, which is important for industrial uses. There was also detected a metallo-carboxypeptidase activity, which has been not described in plants. These peptidases must be isolated to confirm or not these indications. However, these data indicate the biological and technological importance of extending the studies about plant peptidases on a diverse genetic basis.How to cite this paper: Barduche, D., do

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“…APs contain two Asp residues that are crucial for catalytic activity. They are most active under acidic conditions (pH 2-6) and are specifically inhibited by pepstatin A (Mutlu and Gal, 1999;Milisavljevic et al, 2008). Several functions have been proposed for APs, including processing and degradation of storage proteins, protein degradation during organ senescence and cell death, autolysis during the formation of tracheary elements, prey digestion by carnivorous plants, and adhesion-mediated proteolytic mechanisms in pollen recognition and growth (Simões and Faro, 2004).…”

mentioning

confidence: 99%

Misexpression of a Chloroplast Aspartyl Protease Leads to Severe Growth Defects and Alters Carbohydrate Metabolism in Arabidopsis

et al. 2012

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The crucial role of carbohydrate in plant growth and morphogenesis is widely recognized. In this study, we describe the characterization of nana, a dwarf Arabidopsis (Arabidopsis thaliana) mutant impaired in carbohydrate metabolism. We show that the nana dwarf phenotype was accompanied by altered leaf morphology and a delayed flowering time. Our genetic and molecular data indicate that the mutation in nana is due to a transfer DNA insertion in the promoter region of a gene encoding a chloroplast-located aspartyl protease that alters its pattern of expression. Overexpression of the gene (oxNANA) phenocopies the mutation. Both nana and oxNANA display alterations in carbohydrate content, and the extent of these changes varies depending on growth light intensity. In particular, in low light, soluble sugar levels are lower and do not show the daily fluctuations observed in wild-type plants. Moreover, nana and oxNANA are defective in the expression of some genes implicated in sugar metabolism and photosynthetic light harvesting. Interestingly, some chloroplast-encoded genes as well as genes whose products seem to be involved in retrograde signaling appear to be down-regulated. These findings suggest that the NANA aspartic protease has an important regulatory function in chloroplasts that not only influences photosynthetic carbon metabolism but also plastid and nuclear gene expression.

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Two types of aspartic proteinases from buckwheat seed – Gene structure and expression analysis

Cited by 18 publications

References 23 publications

Ubiquitous aspartic proteinase as an actor in the stress response in buckwheat

Ubiquitous aspartic proteinase as an actor in the stress response in buckwheat

Proteolysis in the Subtropical Woody Tree <i>Anadenanthera colubrina</i> (Angico) Seeds during and after Germination

Misexpression of a Chloroplast Aspartyl Protease Leads to Severe Growth Defects and Alters Carbohydrate Metabolism in Arabidopsis

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Two types of aspartic proteinases from buckwheat seed – Gene structure and expression analysis

Cited by 18 publications

References 23 publications

Ubiquitous aspartic proteinase as an actor in the stress response in buckwheat

Ubiquitous aspartic proteinase as an actor in the stress response in buckwheat

Proteolysis in the Subtropical Woody Tree &lt;i&gt;Anadenanthera colubrina&lt;/i&gt; (Angico) Seeds during and after Germination

Misexpression of a Chloroplast Aspartyl Protease Leads to Severe Growth Defects and Alters Carbohydrate Metabolism in Arabidopsis

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Proteolysis in the Subtropical Woody Tree <i>Anadenanthera colubrina</i> (Angico) Seeds during and after Germination