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PubMed2002

Detection of protoporphyrin IX in envelope membranes of pea chloroplasts.

Envelope membranes were prepared from mature pea chloroplasts. The tetrapyrrole contents of envelope membranes were analysed. The envelope membranes of pea chloroplasts contained substantial amounts of protoporphyrin IX and trace amounts of Mg-protoporphyrin IX and its monoester in addition to protochlorophyllide. The protoporphyrin IX content of envelope membranes was 89.25 pmol (mg protein)(-1). Its content in pea envelope membrane was higher than that of protochlorophyllide. The proportion of monovinyl and divinyl forms of protochlorophyllide present in pea chloroplast envelope membrane was 3:7. The significance of the presence of protoporphyrin IX in the envelope membrane is discussed in relation to plastidic Chl biosynthesis.

Chloroplasts↗

PubMed2003

A novel testis-specific RAG2-like protein, Peas: its expression in pachytene spermatocyte cytoplasm and meiotic chromatin.

We report a novel gene Peas that constitutes an overlapping gene complex in mammalian genome. We have cloned human and mouse Peas cDNAs (hPEAS/mPeas) and analyzed their tissue and stage-specific expressions. Peas protein contains six repeated kelch motifs, structurally similar to RAG2, a V(D)J recombination activator, and is evolutionarily conserved among mammals, birds, insects, and nematodes. Northern, RNA in situ hybridization and immunohistochemical analyses showed that mPeas is specifically transcribed in testis, particularly in pachytene spermatocytes in which it is localized to the cytoplasm and meiotic chromatin. It is suggested that Peas may be involved in meiotic recombination process.

Amino Acid Sequence↗

PubMed2003

Food-aid cereals to reduce neurolathyrism related to grass-pea preparations during famine.

Neurolathyrism is a spastic paraparesis that can be caused by excessive consumption of the drought-resistant grass pea (Lathyrus sativus). Devastating neurolathyrism epidemics have occurred during major famine crises in various parts of the world. We investigated in a case-control study the effects of food aid on risk of paralysis. Risk increased with consumption of boiled grass pea (adjusted odds ratio 2.78, 95% CI 1.09-7.13 with cereals; 5.22, 2.01-13.55 without cereal) and raw unripe green grass pea (1.96, 1.16-3.31; p=0.011), but not with the fermented pancake, unleavened bread, and gravy preparations. In a correlational study there was an inverse relation between the number of new cases and the amount of food-aid cereals distributed per person. During famine, cereals and nutritional information should reach people before they have grass pea as the only food.

Case-Control Studies↗

PubMed2000

Four developmental stages identified by genetic dissection of pea (Pisum sativum L.) root nodule morphogenesis.

Root nodule structural organisation of nine pea Fix(-) mutants representing seven symbiotic loci has been studied. This set of mutants has revealed lesions at four developmental stages in the pea-Rhizobium symbiosis. (i) Mutant RisFixA is affected in infection thread differentiation in nodule tissue, infection droplet formation, bacteroid differentiation and nodule persistence. (ii) Allelic mutants RisFixL and RisFixO (sym32) are blocked in bacteroid differentiation. (iii) Mutants RisFixM (sym26), RisFixN, RisFixQ (sym27), RisFixT (sym26) show premature degradation of symbiotic structures. (iv) Mutant RisFixV shows similar defects in nodule persistence but, in addition, this mutant is characterised by an abnormal and severe increase in the thickness of infection thread walls during the process of infection thread 'maturation' and senescence. Combining our new data with previously published studies of pea mutant phenotypes has allowed us to create an integrated scheme for the sequential functioning of the late pea symbiotic genes identified and characterised to date.

Journal Article↗

PubMed2001

Thermal treatment improves nutritional quality of pea seeds (Pisum sativum L.) without reducing their hypocholesterolemic properties.

The effects of isoproteic isoenergetic diets containing raw (RP) or extruded (EP) pea (Pisum sativum, cv. Ballet) seed meal on nutritional performance and serum lipids, amino acids and enzyme levels in growing rats were studied in two 15 d feeding experiments. Food intake and growth were greatly reduced in animals fed unsupplemented RP or EP. Both parameters were improved by addition of amino acids to the diets. Growth, apparent N digestibility, biological value and net protein utilisation values for supplemented (SRP) raw peas were however inferior to those for controls whilst with supplemented (SEP) extruded peas the values were similar to control levels. SRP and SEP also greatly reduced serum total cholesterol, LDL (VLDL) and cholesterol/HDL ratio. This may have been linked to the lower plasma lysine:arginine ratio. SRP and SEP increased kidney and adrenal weights and reduced liver weight. SRP stimulate pancreatic growth but SEP did not. Analysis of serum proteins and enzymes suggested these tissue changes did not lead to chronic disruption to gut or systemic metabolism. Extrusion treatment of peas improved their nutritional quality but did not reduce their hypocholesterolemic properties.

Journal Article↗

PubMed2002

Identification of new pisatin demethylase genes (PDA5 and PDA7) in Nectria haematococca and non-Mendelian segregation of pisatin demethylating ability and virulence on pea due to loss of chromosomal elements.

Previous studies have shown that high virulence on pea in Nectria haematococca Mating Population VI is linked to the ability to detoxify the pea phytoalexin, pisatin, via demethylation (Pda). To test this linkage further, a highly virulent Pda(+) isolate (34-18) was used as the recurrent parent in backcrosses to Pda(-) isolates, but most of the progeny were low in virulence on pea, and tetrad analysis gave conflicting ratios for the genetic control of Pda. Southern analysis of 34-18 and progeny showed that 34-18 carries a gene similar to PDA1 (PDA1-2), two new PDA genes, PDA5 and PDA7, and that all three genes can be lost during meiosis. Southern analysis of electrophoretic karyotypes showed that PDA1-2 is on a 1.5-Mb dispensable chromosome in 34-18 and that PDA5 and PDA7 are on a 4.9-Mb chromosome in 34-18 but are found on variably sized chromosomes in progeny. Loss of PDA5 or PDA7 in progeny was not generally associated with morphological phenotypes, except in progeny from some crosses between PDA5 parents. Loss of PDA5 was associated with growth abnormalities in these crosses, suggesting that in some genetic backgrounds at least a portion of the PDA5/PDA7 chromosome is essential for normal growth. All highly virulent progeny had PDA1-2 or a combination of PDA5 and PDA7 while isolates that lacked the three genes were low in virulence, supporting the hypothesis that Pda, or genes linked to PDA genes, are necessary for virulence on pea. However, low virulence isolates with PDA genes were also identified, suggesting that there are pathogenicity genes that can segregate independently of PDA genes.

Chromosome Mapping↗

PubMed2001

PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase.

The ERK 1/2 MAP kinase pathway controls cell growth and survival and modulates integrin function. Here, we report that PEA-15, a protein variably expressed in multiple cell types, blocks ERK-dependent transcription and proliferation by binding ERKs and preventing their localization in the nucleus. PEA-15 contains a nuclear export sequence required for its capacity to anchor ERK in the cytoplasm. Genetic deletion of PEA-15 results in increased ERK nuclear localization with consequent increased cFos transcription and cell proliferation. Thus, PEA-15 can redirect the biological outcome of MAP kinase signaling by regulating the subcellular localization of ERK MAP kinase.

3T3 Cells↗

PubMed2004

Insecticidal components from field pea extracts: soyasaponins and lysolecithins.

Extracts from field peas (Pisum sativum L.) have previously been shown to have a utility to control insect pests. To identify potentially new bioinsecticides in field crops, we describe the fractionation of impure extracts (C8 extracts) derived from protein-rich fractions of commercial pea flour. The activity of separated fractions was determined by a flour disk antifeedant bioassay with the rice weevil [Sitophilus oryzae (L.)], an insect pest of stored products. Bioassay-guided fractionation showed that the triterpenoid saponin fractions were partly responsible for the antifeedant activity of C8 extracts. Soyasaponin I (soyasaponin Bb), isolated from peas and soybeans, and mixtures of soyasaponins, comprised of soyasaponins I-III and isolated from soybeans, were inactive antifeedants, but dehydrosoyasaponin I (the C-22 ketone derivative of soyasaponin I), a minor component found in C8 extracts, was shown to be an active component. Dehydrosoyasaponin I (soyasaponin Be) and soyasaponin VI (soyasaponin betag) coeluted under conditions of silica gel thin-layer chromatography and C18 high-performance liquid chromatography. However, dehydrosoyasaponin I could be isolated from saponin-enriched fractions with a reversed phase column of styrene/divinylbenzene operated at alkaline pH. Phospholipids of the lysolecithin type were also identified in saponin fractions of C8 extracts from peas. Three of the lysolecithins were inactive alone against rice weevils, but mixtures of these phospholipids enhanced the insecticidal activity of dehydrosoyasaponin I.

Animals↗

PubMed2004

Fermentation of seeds of Teff (Eragrostis teff), grass-pea (Lathyrus sativus), and their mixtures: aspects of nutrition and food safety.

Fermentation of pure teff (Eragrostis teff), pure grass-pea (Lathyrus sativus), and their mixtures, 9:1 and 8:2 (teff/grass-pea) has been done at two temperatures (room temperature and 35 degrees C) in duplicate using the strains of Lactobacillus plantarum, for bacterial fermentation, and Aspergillus oryzae and Rhizopus oligosporus in succession for solid-state fungal fermentation as inocula. In addition, the natural or spontaneous and back-slopping methods of bacterial fermentation have been done on the above four substrate groups. The pH and essential amino acid profiles of the different fermentation processes were compared. The back-slopping in teff at a temperature of 35 degrees C gave the sharpest pH drop. All fermentations done at 35 degrees C showed a steeper slope in their pH versus time plot compared to their room temperature counterpart. Fungal fermentation gave an improved amino acid profile for the essential ones in all of the substrate groups, except in pure grass-pea. Fermented teff/grass-pea (8:2) in this fungal fermentation has been found to be quite comparable in essential amino acid profile to an ideal reference protein recommended for children of 2-5 years of age. None of the bacterial fermentations produced a net change in their essential amino acid profile in any of the substrate groups investigated. Solid state fungal fermentation on pure grass-pea using the fungal strains R. oligosporous and A. oryzae in succession has shown that the neurotoxin beta-N-oxalyl-alpha,beta-diaminopropionic acid (beta-ODAP) in grass-pea has been removed by 80% on average for the high-toxin variety and by up to 97% for the low-toxin variety as determined by an improved chromatographic method with bioelectrochemical detection coupled on-line with refractive index detection.

Amino Acids↗

PubMed2004

Characterization of pea vicilin. 1. Denoting convicilin as the alpha-subunit of the Pisum vicilin family.

Vicilin, a major globulin protein of pea that has been described as "extremely heterogeneous in terms of its polypeptide composition", was extracted from pea flour under alkaline conditions and subsequently fractionated by salt under acid conditions. This procedure induced the separation of vicilin into two fractions, which, after purification, were called vicilin 1 degrees and vicilin 2 degrees. Vicilin 2 degrees was seen on SDS-PAGE to contain the third globulin protein of pea, convicilin (a band at approximately 70 kDa). Vicilin fractions were thus characterized using gel electrophoresis, differential scanning calorimetry, circular dichroism, and pH-dependent solubility in order to determine whether the convicilin should in fact be considered as a third separate globulin protein of pea. On the basis of the results obtained it was concluded that this distinct polypeptide of the Pisum vicilin gene family should be further denoted as a subunit of the salt extractable protein vicilin. The definition of vicilin heterogeneity should therefore be extended to acknowledge the possible oligomeric inclusion of the 70 kDa polypeptide that is here denoted as the alpha-subunit.

Calorimetry, Differential Scanning↗

PubMed2004

Heat-induced gelation of pea legumin: comparison with soybean glycinin.

Gel network formation of pea legumin (8.4% on a protein basis, pH 7.6) was monitored via dynamic rheological measurements. Gelation was performed in the absence and presence of the thiol-blocking reagent N-ethylmaleimide, at different rates of heating and cooling. Overall, it was shown that pea legumin gel formation was not effected by changes in the heating rate, and the two differently heated samples were unaffected by the addition of 20 mM NEM, which indicated that disulfide bonds were not essential within the network strands of these legumin gels. However, slowly cooling the legumin samples caused disulfide bonds to become involved within the network; this was observed by a large increase in gel strength that was then substantially reduced when repeating the sample in the presence of NEM. These experiments were repeated with soybean glycinin in order to determine whether a common model for gel formation of legumin-like proteins could be built, based upon molecular reasoning. The two proteins were affected in the same way by changes in the conditions used, but when applying a procedure of reheating and recooling the gel networks responded differently. Pea legumin gel networks were susceptible to rearrangements that caused the gels to become stronger after reheating/recooling, yet glycinin gel networks were not. It was concluded that the same physical and chemical forces drove the processes of denaturation, aggregation, and network formation. Each process can therefore be readily targeted for modification based upon molecular reasoning. Pea legumin and soybean glycinin gel networks had structurally different building blocks, however. A model of gelation aimed at texture control therefore requires additional information.

Ethylmaleimide↗

PubMed2006

Fermented pigeon pea (Cajanus cajan) ingredients in pasta products.

Pigeon pea (Cajanus cajan var. aroíto) seeds were fermented in order to remove antinutritional factors and to obtain functional legume flour to be used as pasta ingredients. Fermentation brought about a drastic reduction of alpha-galactosides (82%), phytic acid (48%), and trypsin inhibitor activity (39%). Fermented legume flours presented a notable increase of fat and total soluble available carbohydrates, a slight decrease of protein, dietary fiber, calcium, vitamin B2, vitamin E, and total antioxidant capacity, and a decrease of soluble dietary fiber, Na, K, Mg, and Zn contents. No changes were observed in the level of starch and tannins as a consequence of fermentation. The fermented flour was used as an ingredient to make pasta products in a proportion of 5, 10, and 12%. The supplemented pasta products obtained had longer cooking times, higher cooking water absorptions, higher cooking loss, and higher protein loss in water than control pasta (100% semolina). From sensory evaluations, fortified pasta with 5 and 10% fermented pigeon pea flour had an acceptability score similar to control pasta. Pasta supplemented with 10% fermented pigeon pea flour presented higher levels of protein, fat, dietary fiber, mineral, vitamin E, and Trolox equivalent antioxidant capacity than 100% semolina pasta and similar vitamins B1 and B2 contents. Protein efficiency ratios and true protein digestibility improved (73 and 6%, respectively) after supplementation with 10% fermented pigeon pea flour; therefore, the nutritional value was enhanced.

Cajanus↗

PubMed1997

Isolation and transcript analysis of gibberellin 20-oxidase genes in pea and bean in relation to fruit development.

PCR was used with degenerate primers based on conserved amino acid sequences in gibberellin (GA) 20-oxidases to isolate cDNA clones for these enzymes from young seeds of pea (Pisum sativum) and developing embryos of French bean (Phaseolus vulgaris). One GA 20-oxidase cDNA (Ps27-12) was obtained from pea and three (Pv 15-11, Pv73-1 and Pv85-26) from bean. Their identities were confirmed by demonstrating that fusion proteins expressed in Escherichia coli exhibited GA 20-oxidase activity, converting [14C]GA12 to [14C]GA9. The intermediates in this three-step reaction, GA15 and GA24, were also identified as products. The expression proteins from three of the clones (Ps27-12, Pv15-11 and Pv73-1) were also shown to convert GA53 to GA20, as effectively as they did GA12. On the basis of transcript levels measured by northern blot analysis, the pea GA 20-oxidase gene is most highly expressed in young leaves, fully expanded internodes, very young seeds (until 4 days after anthesis) and expanding pods (from 3 days after anthesis at least until day 6). Expression in pods from 3-day-old unpollinated ovaries is higher than in those from pollinated ovaries. Treatment of unpollinated ovaries with GA3 to induce parthenocarpic fruit-set severely reduced the amount of GA 20-oxidase mRNA, whereas treatment with 2,4-D, although inducing fruit-set, did not reduce the levels of these transcripts. Plant decapitation above an unpollinated ovary resulted in very high levels of GA 20-oxidase mRNA in the pod. The three GA 20-oxidase genes from French bean showed very different patterns of expression: Pv 15-1 was expressed in the roots, young leaves, and developing seeds, but most highly in immature cotyledons, while Pv73-1 has a similar expression pattern to Ps27-12, with transcripts found only in young seeds and young leaves, where it was particularly abundant. Transcripts corresponding to Pv85-26 were detected in developing seeds, and just traces in the young leaves. Southern blot analysis indicated that the bean GA 20-oxidases are each encoded by single-copy genes, whereas one more gene, homologous to Ps27-12, could also exist in pea.

Amino Acid Sequence↗

PubMed1999

Cloning and characterization of a cDNA encoding topoisomerase II in pea and analysis of its expression in relation to cell proliferation.

We have isolated and sequenced four overlapping cDNA clones to identify the full-length cDNA for topoisomerase II (PsTopII) from pea. Using degenerate primers, based on the conserved amino acid sequences of other eukaryotic type II topoisomerases, a 680 bp fragment was PCR-amplified with pea cDNA as template. This fragment was used as a probe to screen an oligo-dT-primed pea cDNA library. A partial cDNA clone was isolated that was truncated at the 3' end. RACE-PCR was employed to isolate the remaining portion of the gene. The total size of PsTopII is 4639 bp with an open reading frame of 4392 bp. The deduced amino acid sequence shows a strong homology to other eukaryotic topoisomerase II (topo II) at the N-terminus end. The topo II transcript was abundant in proliferative tissues. We also show that the level of topo II transcripts could be stimulated by exogenous application of growth factors that induced proliferation in vitro cultures. Light irradiation to etiolated tissue strongly stimulated the expression of topo II. These results suggest that topo II gene expression is up-regulated in response to light and hormones and correlates with cell proliferation. Besides, we have also isolated and analysed the 5'-flanking region of the pea TopII gene. This is first report on the isolation of a putative promoter for topoisomerase II from plants.

3' Untranslated Regions↗

PubMed2002

The composition of pigeon peas (Cajanus cajan (L.) Millsp.) grown in Botswana.

This study investigated the composition of pigeon peas (Cajanus cajan), grown at Sebele, Botswana. The raw seeds of six varieties were analyzed for dry matter, crude fat, protein, fiber, and ash, using Association of Official Analytical Chemists procedures. Major minerals, Ca, K, P, Mg, Na and trace minerals, Cu, Fe and Zn were also assessed. The range of nutrient contents obtained were: dry matter 86.6-88.0%, crude protein 19.0-21.7%, crude fat 1.2-1.3%, crude fiber 9.8-13.0%, and ash 3.9-4.3%. Minerals ranges (mg/100 g dry matter) were: K 1845-1941, P 163-293, Ca 120-167, Mg 113-127, Na 11.3-12.0, Zn 7.2-8.2, Fe 2.5-4.7 and Cu 1.6-1.8. There were no significant differences in Na among the six varieties (p > 0.05). For the other components, varietal differences (p < 0.05) were observed. The values obtained for the dry matter, crude protein, fat, ash, Ca, Cu, Fe, and Mg were similar to those in pigeon peas grown elsewhere, while those for crude fiber and Zn were higher. In general, the composition of pigeon peas compared favorably with those of other legumes such as Bambara groundnut (Vigna subterranea). The levels of crude protein, crude fiber, K, Ca, P and Mg indicated that pigeon peas could be valuable in the diet of the people of Botswana. This crop would positively contribute protein in the diet and the diversification of agricultural produce.

Botswana↗

PubMed2003

Effect of electron-transport inhibitors on the generation of reactive oxygen species by pea mitochondria during succinate oxidation.

The effect of inhibitors of the cytochrome pathway and alternative oxidase on the rate of respiration and generation of reactive oxygen species by pea mitochondria was studied. Respiration of mitochondria from pea cotyledons was inhibited by 70-80% by salicylhydroxamate (SHAM). The rate of hydrogen peroxide production by pea cotyledon mitochondria during succinate oxidation was 0.15 nmol/min per mg protein. SHAM considerably accelerated the hydrogen peroxide production. The SHAM-dependent H2O2 production was stimulated by 2 micro M antimycin A and inhibited by 5 mM KCN and 1 micro M myxothiazol. The study of the rate of O2*- generation by pea mitochondria using EPR spin traps and epinephrine oxidation showed that H2O2 accumulation can be accounted for by a significant increase in the rate of O2*- production.

Electron Transport↗

PubMed1980

The purification and characterization of a third storage protein (convicilin) from the seeds of pea (Pisum sativum L.).

A third storage protein, distinct from legumin and vicilin, has been purified from the seeds of pea (Pisum sativum L.). This protein has been named 'convicilin' and is present in protein bodies isolated from pea seeds. Convicilin has a subunit mol.wt. of 71 000 and a mol.wt. in its native form of 290 000. Convicilin is antigenically dissimilar to legumin, but gives a reaction of identity with vicilin when tested against antibodies raised against both proteins. However, convicilin contains no vicilin subunits and may be clearly separated from vicilin by non-dissociating techniques. Unlike vicilin, convicilin does not interact with concanavalin A, and contains insignificant amounts of carbohydrates. Limited heterogeneity, as shown by isoelectric focusing, N-terminal analysis, and CNBr cleavage, is present in convicilin isolated from a single pea variety; genetic variation of the protein between pea lines has also been observed.

Amino Acids↗

PubMed1986

The control of CTP:choline-phosphate cytidylyltransferase activity in pea (Pisum sativum L.).

Several possible control mechanisms for CTP:choline-phosphate cytidylyltransferase (EC 2.7.7.15) activity in pea (Pisum sativum L.) stems were investigated. Indol-3-ylacetic acid (IAA) treatment of the pea stems decreased total cytidylyltransferase activity but did not affect its subcellular distribution. Oleate (2 mM) caused some stimulation of enzyme activity by release of activity from the microsomal fraction into the cytosol, but neither phosphatidylglycerol nor monoacyl phosphatidylethanolamine had an effect on activity or subcellular distribution. A decrease in soluble cytidylyltransferase protein concentrations was found in IAA-treated pea stems, but this was not sufficient to account for all of the decrease in cytidylyltransferase activity. A 50% inhibition of enzyme activity could be obtained with 0.2 mM-CMP, which indicated possible allosteric regulation. Similar inhibition was obtained with 1.5 mM-ATP, but other nucleotides had no effect. The cytidylyltransferase enzyme protein was not directly phosphorylated, and the inhibition with 1.5 mM-ATP occurred with the purified enzyme, thus excluding an obligatory mediation via a modulator protein. The results indicate that the cytosolic form of cytidylyltransferase is the most important in pea stem tissue and that the decrease in cytidylyltransferase activity in IAA-treated material appears to be brought about by several methods.

Adenosine Triphosphate↗