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PubMed1992

Mutational analysis of pea lectin. Substitution of Asn125 for Asp in the monosaccharide-binding site eliminates mannose/glucose-binding activity.

As part of a strategy to determine the precise role of pea (Pisum sativum) lectin, Psl, in nodulation of pea by Rhizobium leguminosarum, mutations were introduced into the genetic determinant for pea lectin by site-directed mutagenesis using PCR. Introduction of a specific mutation, N125D, into a central area of the sugar-binding site resulted in complete loss of binding of Psl to dextran as well as of mannose/glucose-sensitive haemagglutination activity. As a control, substitution of an adjacent residue, A126V, did not have any detectable influence on sugar-binding activity. Both mutants appeared to represent normal Psl dimers with a molecular mass of about 55 kDa, in which binding of Ca2+ and Mn2+ ions was not affected. These results demonstrate that the NHD2 group of Asn125 is essential in sugar binding by Psl. To our knowledge, Psl N125D is the first mutant legume lectin which is unable to bind sugar residues. This mutant could be useful in the identification of the potential role of the lectin in the recognition of homologous symbionts.

Amino Acid Sequence↗

PubMed1995

Molecular cloning and expression of mRNAs encoding H1 histone and an H1 histone-like sequences in root tips of pea (Psium sativum L.).

Two cDNA clones representing mRNAs, highly expressed in pea root tips, were isolated by mRNA differential display. Ribonuclease protection analyses showed different patterns of expression of these two messages in several pea tissues. Sequence analysis showed that the first clone, PsH1b-40, has 100% homology with a previously isolated H1 histone cDNA, PsH1b. However, it has an additional 30 nt at the 3' end which is absent in PsH1b, suggesting possible multiple polyadenylation sites in the same mRNA. The second clone, PsH1b-41, encodes a deduced 19.5 kDa protein of 185 amino acids with an isoelectric point of 11.5. The putative globular domain of the encoded protein showed 67-71% residue identity with globular domains of 28 kDa pea PsH1b H1 histone and Arabidopsis thaliana H1-1 H1 histone. It has 9 repeating motifs of (T/S)XXK. In the C-terminal domain, there are four lysine-rich repeating motifs of SXK(T/S)PXKKXK which may be involved in chromatin condensation and decondensation. Southern blot analysis of nuclear DNA shows that PsH1-41 belongs to a multigene family.

Amino Acid Sequence↗

PubMed1995

Repression of the pea lipoxygenase gene loxg is associated with carpel development.

A cDNA clone (loxg) corresponding to a gene repressed during carpel development has been isolated from a cDNA library of unpollinated carpels induced to grow by treatment with gibberellic acid (GA3). The sequences of loxg cDNA and the deduced polypeptide have a high similarity with legume type 2 lipoxygenases, especially with Phaseolus lox1 (78.5% similarity at the protein level) and pea and soybean lox3 (83.6% and 85.4%, respectively). loxg expression is constant in unstimulated carpels but it decreases in carpels induced to keep growing by fertilization or hormone treatment. A similar pattern of repression was observed in lipoxygenase activity of pea and tomato carpels. In situ hybridization studies showed that loxg mRNAs are present in the endocarp and the mesocarp of pea pods; no loxg expression was detectable either in the pod exocarp or in the ovules. Loxg is also expressed in other young growing tissues, especially in flower organs. Nevertheless, the natural pattern of flower and fruit development is associated with loxg repression.

Amino Acid Sequence↗

PubMed1991

Purification and cDNA sequencing of an oleate-selective acyl-ACP:sn-glycerol-3-phosphate acyltransferase from pea chloroplasts.

The soluble acyl-ACP:sn-glycerol-3-phosphate acyltransferase from chloroplasts of chilling-sensitive and -resistant plants differ in their fatty acid selectivity. Enzymes from resistant plants discriminate against non-fluid palmitic acid and select oleic acid whereas the acyltransferase from sensitive plants accepts both fatty acids. To use this difference for improving plant chilling resistance by biotechnology the gene for an oleate-selective enzyme is required. Therefore, the oleate-selective enzyme from pea seedlings was purified to apparent homogeneity. Tryptic peptides of internal origin were sequenced. Polyclonal antibodies raised in rabbits were used for an immunological screening of a pea leaf cDNA expression library in lambda gt11. A positive clone of 1800 bp was selected showing an open reading frame which codes for 457 amino acids. The deduced amino acid sequence coincides perfectly with the tryptic sequences. A tentative assignment of the processing site was made which divides the preprotein into a mature protein of 41 kDa in accordance with experimental findings and a transit peptide of 88 amino acids. At present the comparison between a selective (pea) and an unselective (squash) acyltransferase sequence does not provide a clue for recognizing the structural differences resulting in different selectivities.

1-Acylglycerophosphocholine O-Acyltransferase↗

PubMed1994

Two ABA-responsive proteins from pea (Pisum sativum L.) are closely related to intracellular pathogenesis-related proteins.

We report here the isolation of cDNAs encoding two abscisic acid-responsive pea (Pisum sativum L.) proteins, ABR17 and ABR18, which are synthesized during late seed development in vivo. Southern blot analyses suggest that ABR17 cDNA corresponds to a single-copy gene, but ABR18 is one member of a family of closely related sequences in the pea genome. The deduced amino acid sequences of ABR17 and ABR18 cDNAs showed similarity to those of the pea disease resistance response proteins, to pathogenesis-related and to stress-induced proteins in other species and to the major birch pollen allergen Betv1.

Abscisic Acid↗

PubMed1992

Expression and secretion of pea-seed lipoxygenase isoenzymes in Saccharomyces cerevisiae.

Lipoxygenases (EC 1.13.11.12) catalyse the oxygenation of polyunsaturated fatty acids such as linoleic and arachidonic acid into reactive cis/trans hydroperoxidiene intermediates, which then serve as substrates for other enzymes leading to the production of a variety of secondary metabolites. In order to explore the characteristics of the individual lipoxygenase isoenzymes in more detail larger amounts of the pure enzymes are needed and their production in a heterologous host is therefore desirable. Full-length cDNAs encoding pea-seed lipoxygenase isoenzymes 2 and 3 were expressed in Saccharomyces cerevisiae with the aid of yeast-Escherichia coli shuttle vectors. Expression of the cDNA for lipoxygenase 2 under the control of the constitutive phosphoglycerate kinase (PGK) gene promoter yielded significant amounts of active enzyme inside the cell, both with yeast transformants carrying the cDNA gene on high-copy-number plasmids or integrated in chromosome V. Addition of the yeast invertase signal sequence in front of the pea lipoxygenase 3 yielded secreted active pea-seed lipoxygenase in the medium, but large amounts of inactive lipoxygenase 3 remained inside the yeast cell. Expression of the LOX3 cDNA can be achieved either constitutively with the PGK promoter or inducibly with the GAL1 promoter.

Base Sequence↗

PubMed1989

The plastid rpoA gene encoding a protein homologous to the bacterial RNA polymerase alpha subunit is expressed in pea chloroplasts.

The gene rpoA, encoding a protein homologous to the alpha subunit of RNA polymerase from Escherichia coli has been located in pea chloroplast DNA downstream of the petD gene for subunit IV of the cytochrome b-f complex. Nucleotide sequence analysis has revealed that rpoA encodes a polypeptide of 334 amino acid residues with a molecular weight of 38916. Northern blot analysis has shown that rpoA is co-transcribed with the gene for ribosomal protein S11. A lacZ-rpoA gene-fusion has been constructed and expressed in E. coli. Antibodies raised against the fusion protein have been employed to demonstrate the synthesis of the rpoA gene product in isolated pea chloroplasts. Western blot analysis using these antibodies and antibodies against the RNA polymerase core enzyme from the cyanobacterium, Anabaena 7120, has revealed the presence of the gene product in a crude RNA polymerase preparation from pea chloroplasts.

Amino Acid Sequence↗

PubMed1995

Growth, hormonal status and protein turnover in rats fed on a diet containing peas (Pisum sativum L.) as the source of protein.

The inclusion of peas (Pisum sativum L.) as the source of protein in the diet of growing rats brings about a reduction in growth rate as well as the impairment in the liver, muscle and spleen weights as compared with casein fed controls. Also, a fall in plasma glucose, triglycerides and protein was observed in the legume fed animals, while no changes in cholesterol levels were found. Furthermore, the rats fed on the diet containing peas showed lower levels of plasma insulin, corticosterone, IGF-I and T4 as compared with casein controls. Liver and muscle total protein (mg) and total DNA (mg) were markedly decreased in the legume fed animals, but DNA/g, protein/DNA and RNA/protein ratios were similar in both dietary groups. Likewise, liver and muscle fractional synthesis rates were similar in the casein and legume groups, while the whole body protein synthesis is assumed to be lower in the legume fed animals due to differences in body weights. It is concluded that animals fed on a diet containing peas (Pisum sativum L.) as the only source of protein showed less adverse effects than those found with other legumes such as Vicia faba L. or Phaseolus vulgaris L., in which protein quality, antinutritional factors and nutrient availability could be involved.

Animals↗

PubMed1993

Miso from peas (Pisum sativum) and beans (Phaseolus vulgaris) of domestic origin. Fermented foods from agricultural products in Europe. II.

Miso is a fermented soybean paste widely used in Japan as a soup base or as a seasoning agent. Koji (cereal grains with the mold Aspergillus oryzae) serves as enzyme source. Peas (Pisum sativum) and beans (Phaseolus vulgaris) of German origin can be used as substitutes for soybeans in the preparation of miso-like products. The legumes (peas, beans and soybeans for comparison) are washed, soaked in boiled water, dehulled and cooked for 35 min at reduced pressure. After grounding the seeds are mixed with salt, koji and mugi miso as starter and incubated at 45 degrees C for 14 days. During fermentation the glucose content increases up to 8-10 days and subsequently drops down. Crude protein decreases during incubation while dry matter increases. The pH value of all three miso types decreases during the fermentation period. Most of the 40 test persons characterize odor and flavor of the three misos as aromatic or sour; pea miso is often recorded to have a sweet-like odor and flavor. A legume-like taste of the final products has not been recorded.

Fabaceae↗

PubMed1994

Detection of a 45 kD protein derived from the N terminus of the pea seedborne mosaic potyvirus polyprotein in vivo and in vitro.

A 45 kD protein (Pro1) derived from the N terminus of the pea seedborne mosaic potyvirus (PSbMV) polyprotein has been detected in extracts of infected pea plants and among in vitro translation products of PSbMV genomic RNA. The genomic region coding for the first 231 amino acids of the PSbMV polyprotein was cloned and expressed in Escherichia coli as a fusion protein with beta-galactosidase. A rabbit antiserum raised against the fusion protein recognized an approximately 45 kD protein in immunoblots of extracts of PSbMV-infected pea leaves that was not present in extracts of healthy leaves. The highest concentration of the 45 kD protein was found in extracts of young leaves, suggesting the protein may be rapidly degraded in vivo. After in vitro translation of PSbMV genomic RNA in a wheat germ extract, the antiserum immunoprecipitated a 45 kD polypeptide as well as some lower molecular weight translation products. On the other hand, an approximately 90 kD polypeptide was immunoprecipitated from in vitro translation products of genomic RNA in a rabbit reticulocyte lysate, corresponding to the combined molecular weights of Pro1 and the helper component predicted from genomic sequence data.

Binding Sites↗

PubMed2002

Mapping of the nodulation loci sym9 and sym10 of pea ( Pisum sativum L.).

Several mutants defective in the nodulation process during rhizobial or endomycorrhizal endosymbiosis of pea have been identified previously. We have integrated the map positions of two such nodulation mutations, sym9 and sym10, into the molecular map of pea by applying molecular-marker techniques combined with bulked segregant analysis (BSA). Lines P2 and P54 were found to carry alleles of sym9, line P56 carried an allele of sym10. F2 populations were derived from crosses of P2, P54 and P56, to JI281 and JI15, two of the parental lines that have been used previously to generate a molecular map of pea. sym9 was located on linkage group IV by AFLP-BSA analysis and subsequently mapped by RFLP in both F2 populations, P2 x JI281 and P54 x JI281. RFLP-BSA analysis was applied to assign sym10 to linkage group I. The RFLP marker locus, chs2, co-segregates with sym10 in the F2 population of P56 x JI15.

Journal Article↗

PubMed2004

Mapping of quantitative trait loci for partial resistance to Mycosphaerella pinodes in pea (Pisum sativum L.), at the seedling and adult plant stages.

The inheritance of resistance to Ascochyta blight, an economically important foliar disease of field pea ( Pisum sativum L.) worldwide, was investigated. Breeding resistant pea varieties to this disease, caused by Mycosphaerella pinodes, is difficult due to the availability of only partial resistance. We mapped and characterized quantitative trait loci (QTLs) for resistance to M. pinodes in pea. A population of 135 recombinant inbred lines (RILs), derived from the cross between DP (partially resistant) and JI296 (susceptible), was genotyped with morphological, RAPD, SSR and STS markers. A genetic map was elaborated, comprising 206 markers distributed over eight linkage groups and covering 1,061 cM. The RILs were assessed under growth chamber and field conditions at the seedling and adult plant stages, respectively. Six QTLs were detected at the seedling stage, which together explained up to 74% of the variance. Ten QTLs were identified at the adult plant stage in the field, and together these explained 56.6-67.1% of the variance, depending on the resistance criteria and the organ considered. Four QTLs were detected under both growth chamber and field conditions, suggesting they were not plant-stage dependent. Three QTLs for flowering date and three QTLs for plant height were also identified in the RIL population, some of which co-located with QTLs for resistance. The relationship between QTLs for resistance to M. pinodes, plant height and flowering date is discussed.

Analysis of Variance↗

PubMed2004

Identification of markers tightly linked to sbm recessive genes for resistance to Pea seed-borne mosaic virus.

Two virus resistance loci on linkage groups II and VI have provided the only sources of natural resistance against Pea seed-borne mosaic virus (PSbMV, Potyviridae) in the important crop plant Pisum sativum L. A combination of parallel approaches was used to collate linked markers, particularly for sbm-1 resistance on linkage group VI. We have identified sequences derived from the genes for the eukaryotic translation initiation factors eIF4E and eIF(iso)4E as being very tightly linked to the resistance gene clusters on linkage groups VI and II, respectively. In particular, no recombinants between sbm-1 and eIF4E were found amongst 500 individuals of an F2 cross between the BC4 resistant line (JI1405) and its recurrent susceptible parent 'Scout'. In a different mapping population, the gene eIF(iso)4E was also shown to be linked to sbm-2 on linkage group II. A parallel cDNA-AFLP comparison of pairs of resistant and susceptible lines also identified an expressed tag marker just 0.7 cM from sbm-1. eIF4E and eIF(iso)4E have been associated with resistance to related viruses in other hosts. This correlation strengthens the use of our markers as valuable tools to assist in breeding multiple virus resistances into peas, and identifies potential targets for resistance gene identification in pea.

Agriculture↗

PubMed2006

Functional mapping in pea, as an aid to the candidate gene selection and for investigating synteny with the model legume Medicago truncatula.

The identification of the molecular polymorphisms giving rise to phenotypic trait variability-both quantitative and qualitative-is a major goal of the present agronomic research. Various approaches such as positional cloning or transposon tagging, as well as the candidate gene strategy have been used to discover the genes underlying this variation in plants. The construction of functional maps, i.e. composed of genes of known function, is an important component of the candidate gene approach. In the present paper we report the development of 63 single nucleotide polymorphism markers and 15 single-stranded conformation polymorphism markers for genes encoding enzymes mainly involved in primary metabolism, and their genetic mapping on a composite map using two pea recombinant inbred line populations. The complete genetic map covers 1,458 cM and comprises 363 loci, including a total of 111 gene-anchored markers: 77 gene-anchored markers described in this study, 7 microsatellites located in gene sequences, 16 flowering time genes, the Tri gene, 5 morphological markers, and 5 other genes. The mean spacing between adjacent markers is 4 cM and 90% of the markers are closer than 10 cM to their neighbours. We also report the genetic mapping of 21 of these genes in Medicago truncatula and add 41 new links between the pea and M. truncatula maps. We discuss the use of this new composite functional map for future candidate gene approaches in pea.

Chromosome Mapping↗

PubMed2005

Characterization of a facultative endosymbiotic bacterium of the pea aphid Acyrthosiphon pisum.

The pea aphid U-type symbiont (PAUS) was investigated to characterize its microbiological properties. Fluorescence in situ hybridization (FISH) and electron microscopy revealed that PAUS was a rod-shaped bacterium found in three different locations in the body of the pea aphid Acyrthosiphon pisum: sheath cells, secondary mycetocytes, and hemolymph. Artificial transfer experiments revealed that PAUS could establish stable infection and vertical transmission when introduced into uninfected pea aphids. When 28 aphid species collected in Japan were subjected to a diagnostic PCR assay, four species of the subfamily Aphidinae (Aphis citricola, Aphis nerii, Macrosiphum avenae, and Uroleucon giganteus) and a species of the subfamily Pemphiginae (Colopha kansugei) were identified to be PAUS-positive. The sporadic incidences of PAUS infection without reflecting the aphid phylogeny can be best explained by occasional horizontal transfers of the symbiont across aphid lineages.

Animals↗

PubMed2003

Influence of Agrobacterium tumefaciens strain on the production of transgenic peas ( Pisum sativum L.).

We compared the efficiency of two Agrobacterium tumefaciens strains, AGL 1 and KYRT1, for producing transgenic pea plants. KYRT1 is a disarmed strain of Chry5 that has been shown to be highly tumourigenic on soybean. The efficacies of the strains were compared using cotyledon explants from three pea genotypes and two plasmids. The peas were sourced from field-grown plants over three Southern Hemisphere summer seasons. Overall, KYRT1 was found to be on average threefold more efficient than AGL 1 for producing transgenic plants. We suggest that KYRT1 is sensitive to cocultivation temperature as the expected increase in efficiency was not achieved at high laboratory temperatures.

Agrobacterium tumefaciens↗

PubMed2002

Hormone levels and response during de-etiolation in pea.

The objective of this study was to increase our understanding of the hormonal regulation of de-etiolation by investigating endogenous hormone levels and response in etiolated pea ( Pisum sativum L.) seedlings after exposure to continuous white light. Recent reports suggest that de-etiolation may result from the down-regulation of an enzyme in the brassinosteroid (BR) biosynthesis pathway in pea. A subsequent review highlighted the need for direct measurements of BR levels to support this hypothesis. We have shown that endogenous castasterone and 6-deoxocastasterone levels are not greatly reduced after exposure to light; indeed, 6-deoxocastasterone levels were actually increased. Similarly, the elongation response to exogenous brassinolide was greater in plants grown in continuous light, or in dark-grown plants that had been transferred into the light, than in plants that were grown in continuous darkness. These results provide further evidence to suggest that BRs do not negatively regulate de-etiolation in pea. However, changes in the levels of several other hormones have also been implicated in light-regulated development. We have simultaneously quantified indole-3-acetic acid (IAA), gibberellin (GA), and abscisic acid levels in whole seedlings, which revealed a complex pattern of changes in the levels of these substances after exposure to light. The first and most dramatic of these changes was a significant reduction in GA(1) levels, which reached a minimum 8 h after exposure to light. Whilst GA(1) levels rapidly decreased, IAA levels remained unchanged in the short term after exposure to light, suggesting that GA(1) levels may be the primary factor regulating the reduction in elongation growth during de-etiolation. In the long term after exposure to light, IAA levels underwent a transitory increase, which peaked at 48 h, and had abated by 96 h. However, abscisic acid levels remained unchanged in the first 1 h after exposure to light before undergoing a steady decline over time. The relative importance of these changes in mediating light-induced changes in plant morphology is discussed.

Abscisic Acid↗

PubMed2004

The pea END1 promoter drives anther-specific gene expression in different plant species.

END1 was isolated by an immunosubtractive approach intended to identify specific proteins present in the different pea (Pisum sativum L.) floral organs and the genes encoding them. Following this strategy we obtained a monoclonal antibody (mAbA1) that specifically recognized a 26-kDa protein (END1) only detected in anther tissues. Northern blot assays showed that END1 is expressed specifically in the anther. In situ hybridization and immunolocalization assays corroborated the specific expression of END1 in the epidermis, connective, endothecium and middle layer cells during the different stages of anther development. END1 is the first anther-specific gene isolated from pea. The absence of a practicable pea transformation method together with the fact that no END1 homologue gene exists in Arabidopsis prevented us from carrying out END1 functional studies. However, we designed functional studies with the END1 promoter in different dicot species, as the specific spatial and temporal expression pattern of END1 suggested, among other things, the possibility of using its promoter region for biotechnological applications. Using different constructs to drive the uidA (beta-glucuronidase) gene controlled by the 2.7-kb isolated promoter sequence we have proven that the END1 promoter is fully functional in the anthers of transgenic Arabidopsis thaliana (L.) Heynh., Nicotiana tabacum L. (tobacco) and Lycopersicon esculentum Mill. (tomato) plants. The presence in the -330-bp region of the promoter sequence of three putative CArG boxes also suggests that END1 could be a target gene of MADS-box proteins and that, subsequently, it would be activated by genes controlling floral organ identity.

Amino Acid Sequence↗