Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “PEAS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 847 records · Page 47Linked to original sources

Development of an efficient retrotransposon-based fingerprinting method for rapid pea variety identification.

Fast and efficient DNA fingerprinting of crop cultivars and individuals is frequently used in both theoretical population genetics and in practical breeding. Numerous DNA marker technologies exist and the ratio of speed, cost and accuracy are of importance. Therefore even in species where highly accurate and polymorphic marker systems are available, such as microsatellite SSR (simple sequence repeats), also alternative methods may be of interest. Thanks to their high abundance and ubiquity, temporary mobile retrotransposable elements come into recent focus. Their properties, such as genome wide distribution and well-defined origin of individual insertions by descent, predetermine them for use as molecular markers. In this study, several Ty3-gypsy type retrotransposons have been developed and adopted for the inter-retrotransposon amplified polymorphism (IRAP) method, which is suitable for fast and efficient pea cultivar fingerprinting. The method can easily distinguish even between genetically closely related pea cultivars and provide high polymorphic information content (PIC) in a single PCR analysis.

Breeding↗

Quantitative trait loci for partial resistance to Aphanomyces root rot in pea.

Aphanomyces root rot, caused by Aphanomyces euteiches Drechs, is the most-important disease of pea ( Pisum sativum L.) worldwide. No efficient chemicals are available to control the pathogen. To facilitate breeding for Aphanomyces root rot resistance and to better understand the inheritance of partial resistance, our goal was to identify QTLs associated with field partial resistance. A population of 127 RILs from the cross Puget (susceptible) x 90-2079 (partially resistant) was used. The lines were assessed for resistance to A. euteiches under field conditions at two locations in the United States (Pullman, Wash. and LeSueur, Minn.) in 1996 and 1998 for three criteria based on symptom intensity and disease effects on the whole plant. The RILs were genotyped using automated AFLPs, RAPDs, SSRs, ISSRs, STSs, isozymes and morphological markers. The resulting genetic map consisted of 324 linked markers distributed over 13 linkage groups covering 1,094 cM (Kosambi). Twenty seven markers were anchored to other published pea genetic maps. A total of seven genomic regions were associated with Aphanomyces root rot resistance. The first one, located on LG IVb and named Aph1, was considered as "major" since it was highly consistent over the years, locations and resistance criteria studied, and it explained up to 47% of the variation in the 1998 Minnesota trial. Two other year-specific QTLs, namely Aph2 and Aph3, were revealed from different scoring criteria on LG V and Ia, respectively. Aph2 and Aph3 mapped near the r (wrinkled/round seeds) and af (normal/afila leaves) genes, and accounted for up to 32% and 11% of the variation, respectively. Four other "minor" QTLs, identified on LG Ib, VII and B, were specific to one environment and one resistance criterion. The resistance alleles of Aph3 and the two "minor" QTLs on LG Ib were derived from the susceptible parent. Flanking markers for the major Aphanomyces resistance QTL, Aph1, have been identified for use in marker-assisted selection to improve breeding efficiency.

Chromosome Mapping↗

Validation of quantitative trait loci for Ascochyta blight resistance in pea ( Pisum sativum L.), using populations from two crosses.

Resistance to Ascochyta blight of pea was genetically characterized by mapping quantitative trait loci (QTLs) using two crosses, 3147-A26 (A26, partially resistant) x cultivar Rovar (susceptible) and 3148-A88 (A88, partially resistant) x Rovar, with the aim of developing an increased understanding of the genetics of resistance and of identifying linked molecular markers that may be used to develop resistant germplasm. Molecular linkage maps for both crosses were aligned so that the results of QTL mapping could be compared. Ascochyta blight disease severity in response to natural epidemics was measured in field trials conducted in Western Australia and New Zealand. Eleven putative QTLs for Ascochyta blight resistance were identified from the A26 x Rovar population and 14 putative QTLs from the A88 x Rovar population. Six QTLs were associated with the same genomic regions in both populations. These QTLs reside on linkage groups II, III, IV, V, and VII (two QTLs). The severity of Ascochyta blight disease symptoms on pea increases during field epidemics as plants mature; therefore, QTLs for plant reproductive maturity were mapped. Six QTLs were detected for plant maturity in the A26 x Rovar population, while five plant maturity QTLs were mapped in the A88 x Rovar population. QTLs for plant maturity coincide with Ascochyta blight resistance QTLs in four genomic regions, on linkage groups II (two regions), III, and V. The plant maturity and Ascochyta blight resistance QTLs on III were linked in repulsion phase. Therefore, the coincidence of these QTLs may be explained by linkage of distinct loci for the two traits. The QTLs on linkage groups II and V were linked in coupling phase; therefore, linked QTLs for resistance and maturity may be present in these regions, or the Ascochyta blight resistance QTLs detected in these regions are the result of pleiotropic effects of plant-maturity genetic loci.

Ascomycota↗

Polysaccharides of pseudomonas pathovar strains that infect pea, tomato, and soya bean.

In order to understand the mode of action of taxonomically related Pseudomonas syringae pathovar strains that infect pea, tomato, and soya bean, we examined their extracellular polysaccharides (EPS). Maximum production of polysaccharide in shake culture of these pathogens was observed between 24 and 60 h. P. syringae pv. pisi 519, the bacterial blight pathogen of pea, produced a higher amount of polysaccharide (34.87 microg/mL) at 60 h compared with 32.67 microg/mL produced by P. syringae pv. glycinea NCPPB 1783, the bacterial blight pathogen of soya bean, and 30.03 microg/mL produced by P. syringae pv. tomato NCPPB 269, the bacterial speck pathogen of tomato. EPS produced by P. syringae pv. pisi 519, P. syringae pv. tomato NCPPB 269, and P. syringae pv. glycinea NCPPB 1783 was characterized with infrared (FTIR), nuclear magnetic resonance (NMR), high performance thin layer chromatography, (HPTLC), and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. HPTLC profiles revealed the presence of glucose and glucuronic acid in all bacteria and mannose only in P. syringae pv. tomato. Molecular mass of EPS of P. syringae pv. pisi (m/z 933.8), P. syringae pv. tomato (m/z 950.4), and P. syringae pv. glycinea (m/z 933.5) was confirmed by MALDI-TOF mass spectrometry.

Fabaceae↗

A new rickettsia from a herbivorous insect, the pea aphid Acyrthosiphon pisum (Harris).

An undescribed, maternally heritable, rod-shaped bacterium (or "tertiary symbiont") was detected by microscopy in hemolymph of about half (59/122) of pea aphid [Acyrthosiphon pisum (Harris)] clones collected from widely separated locations in California. On the basis of molecular phylogenetic analysis of 16S rDNA sequences, the bacterium was clearly placed among other Rickettsia in the alpha-subgroup of Proteobacteria, close to Rickettsia bellii-a rickettsia found in ticks. A PCR assay was developed to detect this bacterium in pea aphid clones with specific 16S rDNA PCR primers. Results of PCR-based assays completely correlated with detection by microscopy. This is the first confirmed detection of a Rickettsia in a herbivorous insect.

Animals↗

A rooting procedure for lentil (Lens culinaris Medik.) and other hypogeous legumes (pea, chickpea and Lathyrus) based on explant polarity.

The present study assessed the rooting response of lentil nodal segments in relation to explant polarity, hormone, salt and carbohydrate concentrations of the medium. Nodal segments of lentil with an axillary bud cultured in an inverted orientation (apical end in medium) showed higher rooting frequencies than explants cultured in a normal orientation (basal end in medium). The highest rooting percentage (95.35%) and average number of shoots regenerated per explant (2.4) were obtained from explants placed in an inverted orientation on Murashige and Skoog (MS) medium salts with 3% sucrose, supplemented with 5 microM indole acetic acid (IAA) and 1 microM kinetin (KN). Reducing or increasing phytohormone concentration did not alter significantly root regeneration of inverted explants. Sucrose at 3% allowed higher root regeneration frequencies compared to 1.5% sucrose. MS full concentration permitted regeneration of longer shoots with more nodes per regenerated shoot, compared to MS half-strength, which regenerated more shoots of shorter length and with less nodes. Inverted nodal segments of other hypogeous legumes (pea, chickpea and Lathyrus) also exhibited higher rooting frequencies than explants cultured in a normal orientation on MS medium with 3% sucrose and supplemented with 5 microM IAA and 1 microM KN. The most novel application of this study is the culture of nodal segments of hypogeous legumes in an inverted orientation. This procedure is a considerable improvement over other published procedures concerning in vitro rooting of lentil, pea, chickpea and Lathyrus.

Adenine↗

Assignment of linkage groups to pea chromosomes after karyotyping and gene mapping by fluorescent in situ hybridization.

Chromosomes of the pea (Pisum sativum L.) were submitted to fluorescent in situ hybridization (FISH) with probes specific for the oligonucleotides (AG)12, (AC)12, (GAA)10, and (GATA)7 and for the genes encoding 25S rRNA, 5S rRNA and the storage proteins legumin A, K and vicilin. A fourth 5S rRNA gene locus, apparently specific for an accession of the cultivar Grüne Victoria, was newly detected. This allowed all seven chromosome pairs to be distinguished by FISH signals of rRNA genes. The same was possible using a combination of oligonucleotide probes or of oligonucleotides and rRNA gene-specific probes in multicolour FISH. Rehybridization with the 5S rRNA gene-specific probe allowed us to assign vicilin genes to the short arm of chromosome 5, the single legumin A locus to the long arm of chromosome 3 and the legumin B-type genes (exemplified by legumin K) to one locus on the short arm of chromosome 6. Correlation of these data with an updated version of the pea genetic map allowed the assignment of most linkage groups to defined chromosomes. It only remains to be established which of linkage groups IV and VII corresponds to the satellited chromosomes 4 or 7, respectively.

Chromosome Mapping↗

Biosynthesis and cell-wall deposition of a pectin-xyloglucan complex in pea.

Golgi-enriched enzyme preparations prepared from etiolated pea epicotyls incorporated [U-(14)C]galactose from UDP-[U-(14)C]galactose into the 1,4-beta-galactan sidechains of a pectin-xyloglucan complex. This complex could bind to paper and was degraded both by pectin-degrading enzymes and by a xyloglucan-specific endoglucanase. Gel permeation chromatography was used to assess the molecular size of the complex and of enzymically-degraded, galactan-containing fragments of it. Etiolated pea stems were labelled with [U-(14)C]sucrose for 1 h, and the newly-synthesised cell wall polysaccharides were extracted with EDTA or NaOH and fractionated by ion-exchange chromatography. The NaOH-extracted, acidic radioactive polysaccharides obtained in this way were also degraded both by pectin-degrading enzymes and by xyloglucan-specific endoglucanase. Analysis of the radioactive sugar composition indicated that neutral sugars characteristic of both pectin and xyloglucan were present. Analysis of the total non-radioactive, neutral sugar composition of the NaOH-extracted, acidic cell-wall polysaccharides indicated that pectin-xyloglucan complexes were a general feature of the cell wall in this tissue.

Cell Wall↗

NADPH recycling systems in oxidative stressed pea nodules: a key role for the NADP+ -dependent isocitrate dehydrogenase.

The symbiosis between legumes and rhizobia is characterised by the formation of dinitrogen-fixing root nodules. In natural conditions, nitrogen fixation is strongly impaired by abiotic stresses which generate over-production of reactive oxygen species. Since one of the nodule main antioxidant systems is the ascorbate-glutathione cycle, NADPH recycling that is involved in glutathione reduction is of great relevance under stress conditions. NADPH is mainly produced by glucose 6-phosphate dehydrogenase (G6PDH; EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (6PGDH; EC 1.1.1.44) from the oxidative pentose phosphate pathway, and also by NADP(+)-dependent isocitrate dehydrogenase (ICDH; EC 1.1.1.42). In this work, 10 microM paraquat (PQ) was applied to pea roots in order to determine the in vivo relationship between oxidative stress and the activity of the NADPH-generating enzymes in nodules. Whereas G6PDH and 6PGDH activities remained unchanged, a remarkable induction of ICDH gene expression and a dramatic increase of the ICDH activity was observed during the PQ treatment. These results support that ICDH has a key role in NADPH recycling under oxidative stress conditions in pea root nodules.

Carbon↗

Protein- and pH-dependent binding of nascent pectin and glucuronoarabinoxylan to xyloglucan in pea.

Nascent pectin and glucuronoarabinoxylan, synthesised in vitro by membrane-bound enzymes from etiolated pea (Pisum sativum L.) epicotyls, were found to bind to pea xyloglucan in a pH-dependent manner. The binding was maximum at low pH (3-4), and decreased to almost zero at pH 6. The binding was probably non-covalent and reached saturation within 5 min. Removal of the fucose residues of xyloglucan decreased the degree of binding. Removal by protease of the proteins attached to nascent pectin and glucuronoarabinoxylan greatly reduced the maximum binding and abolished the pH-dependence. The observed binding may be of considerable significance in the process of cell-wall assembly and in the control of cell extension.

Binding Sites↗

A cDNA encoding 3-deoxy-D-manno-oct-2-ulosonate-8-phosphate synthase of Pisum sativum L. (pea) functionally complements a kdsA mutant of the Gram-negative bacterium Salmonella enterica.

Recombinant plasmids encoding 3-deoxy-D-manno-oct-2-ulosonate-8-phosphate (Kdo-8-P) synthase (KdsA; EC 4.1.2.16) were identified from a cDNA library of Pisum sativum L. (pea) by complementing a temperature-sensitive kdsA(ts) mutant of the Gram-negative bacterium Salmonella enterica. Sequence analysis of several inserts revealed a central open reading frame encoding a protein of 290 amino acids with a high degree of amino acid sequence similarity to bacterial KdsA. The cDNA was confirmed by amplifying a 1,812-bp DNA fragment from the chromosome of pea that encoded four exons around the 5'-end of kdsA. The recombinant enzyme was subcloned, overexpressed and characterized to synthesize Kdo-8-P from D-arabinose-5-phosphate and phosphoenolpyruvate. The pH optimum was 6.1 and the activity of the enzyme was neither stimulated by the addition of divalent cations nor inhibited by EDTA. The cDNA of kdsA could not complement Escherichia coli K-12 strain AB3257, which is defective in all three isoenzymes (AroFGH) of 3-deoxy-D-arabino-hept-2-ulosonate-7-phosphate (Dha-7-P) synthase (EC 4.1.2.15), and neither D-erythrose-4-phosphate nor D-ribose-5-phosphate could substitute for D-arabinose-5-phosphate in vitro. Thus, plant cells possess a specific enzyme for the biosynthesis of Kdo-8-P with remarkable structural and functional similarities to bacterial KdsA proteins.

Aldehyde-Lyases↗

Flow cytometry, sorting and immunocharacterization with proliferating cell nuclear antigen of cycling and non-cycling cells in synchronized pea root tips.

In the 3-d-old 2-mm root tip of Pisum sativum L. cv. Lincoln the percentage of actively proliferating cells is estimated to be 70%. The remaining cells are non-cycling and arrested with 2C and 4C DNA content in G0 and in G2Q, respectively. In this work we studied the kinetic significance of these quiescent cells, using the sorting capabilities of flow cytometry and immunofluorescence techniques to detect the proliferation marker PCNA (proliferating cell nuclear antigen) inside cells within the different cell-cycle compartments. While in animal cells, PCNA is present at a high level only in actively proliferating cells, in 3-d-old pea root tips 95% of the cells are PCNA-positive. After flow cytometry and sorting of pea non-cycling nuclear populations, all G2Q nuclei appeared strongly PCNA-positive, indicating that these cells had recently left the cell cycle. By contrast, most G0 nuclei showed a low level of PCNA immunofluorescence intensity, as measured by image analysis, with about 25% of the nuclei being PCNA-negative. This small percentage was found to correspond to root cap cells, as could be observed in the root tip section. These are the only cells in the root apical region which are fully differentiated and which, therefore, lack the competence to enter the cell cycle. In contrast, the more or less PCNA-positive G0 nuclei could represent a kinetically heterogeneous population of cells competent to proliferate, but which have either recently left the cell cycle or are progressing to the G0-G1 transition.

Cell Cycle↗

Identification of proteins associated with plastoglobules isolated from pea (Pisum sativum L.) chloroplasts.

Plastoglobules are conspicuous lipid-containing structures in the chloroplast stroma and are thought to serve as lipid reservoirs for thylakoid membranes. Plastoglobules also contain low levels of proteins. We have purified plastoglobules from a pea chloroplast membrane fraction. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis of the purified plastoglobules revealed more than a dozen distinct polypeptides that we propose to term plastoglobulins. For one of the proteins, termed plastoglobulin 1 (PG1), we have obtained partial N-terminal and internal protein sequences. The amino acid sequence, deduced from cDNA, encoded a precursor protein of a calculated mass of 38,491 Da which contained a 48-residue-long N-terminal signal sequence. Pre-PG1 obtained by coupled in-vitro transcription/translation was imported into pea chloroplasts, its signal sequence was cleaved and mature PG1 was assembled into plastoglobules. Homology searches of the data bases revealed similarity of PG1 to the plastoglobule-associated protein of Capsicum annuum, the carotenoid-associated protein of Cucumis sativus and to a protein of the cyanobacterium Synechocystis sp., indicating that PG1 is a novel member of an ancient protein family. Immunoelectron microscopy using PG1 specific antibodies indicated that PG1 is present in multiple copies on the surface of plastoglobules.

Amino Acid Sequence↗

Distinct ethylene- and tissue-specific regulation of beta-1,3-glucanases and chitinases during pea seed germination.

The expression of beta-1,3-glucanase (betaGlu) and chitinase (Chn) was investigated in the testa, cotyledons, and embryonic axis of germinating Pisum sativum L. cv. 'Espresso generoso' seeds. High concentrations of betaGlu and Chn activity were found in the embryonic axis. Treatment with ethylene alone or in combination with the inhibitor of ethylene action 2,5-norbornadiene showed that an early, 4-fold induction of betaGlu activity in the embryonic axis during the first 20 h after the start of imbibition is ethylene-independent. This initial increase was followed by a later 4-fold ethylene-dependent induction in the embryonic axis starting at 50 h, which is after the onset of ethylene evolution and after completion of radicle emergence. The betaGlu activity in cotyledons increased gradually throughout germination and was ethylene-independent. In contrast, the ethylene-independent Chn activity increased slightly after the onset of radical emergence in the embryonic axis and remained at a constant low level in cotyledons. Immunoinactivation assays and immunoblot analyses suggest that early betaGlu activity in the embryonic axis is due to a 54-kDa antigen, whereas late induction is due to a 34.5-kDa antigen, which is likely to be the ethylene-inducible class I betaGlu G2 described for immature pea pods. Increases in Chn in the embryonic axis were correlated with a 26-kDa antigen, whereas amounts of the additional 32- and 20-kDa antigens remained roughly constant. Thus, ethylene-dependent and ethylene-independent pathways regulate betaGlu and Chn during pea seed germination. The pattern of regulation differs from that of leaves and immature pods, and from that described for germinating tobacco seeds. The functional significance of this regulation and its underlying mechanisms are discussed.

Journal Article↗

A 70-kDa chloroplast DNA polymerase from pea ( Pisum sativum) that shows high processivity and displays moderate fidelity.

A 70-kDa chloroplast (ct) DNA polymerase from pea has been purified to apparent homogeneity. The ct DNA polymerase was insensitive to dideoxynucleotides (d(2) NTP) but showed high sensitivity to phosphonoacetic acid. The enzyme lacked any detectable 5'-->3' exonuclease activity but showed 3'-->5' exonuclease activity. The polymerase displayed high processivity (3 kb) and moderate fidelity, which may be sufficient for the faithful replication of the 140-kb pea ct genome. A 43-kDa accessory protein increased the polymerization rate but did not affect the rate of mis-incorporation in vitro, thus indicating that the domains for polymerisation and proof reading may be spatially separate.

Base Sequence↗

Isolation and characterization of a phospholipase C delta isoform from pea that is regulated by light in a tissue specific manner.

Phosphoinositide-specific phospholipases C (PLCs) play an important role in many cellular responses and are involved in the production of secondary messengers. We report the cloning and characterization of a cDNA encoding a PLC-delta from Pisum sativum (PsPLC). The amino acid sequence deduced from the cDNA sequence showed 75-80% identity to other plant PLCs and contained the characteristic X, Y and C2 domains. The genomic PLC clone from pea was also characterized and found to contain eight introns. The protein was expressed in Escherichia coli, but the recombinant product did not show any phosphoinositide (PI)- or phosphatidylinositol-4, 5-bisphosphate (PIP2)-specific activity, despite having all known residues required for such activity, and in spite of the fact that its C2 domain was shown to bind calcium. Under similar in vitro assay conditions the recombinant tobacco PLC used as a control showed calcium-dependent PI- and PIP2-specific activity. Though PsPLC did not show enzyme activity in vitro, and may represent an inactive form of PLC, such as those reported in some mammalian systems, analysis of the transcription of PsPLC showed that the gene is expressed in all pea tissues, and is regulated by light in a tissue-specific manner. Roots showed higher expression of PsPLC than shoots. A putative PsPLC promoter region (792 bp) was also cloned and found to contain root-specific and light-responsive cis elements, suggesting that this form of PLC may be involved in important functions in plants.

Amino Acid Sequence↗

The pea (Pisum sativum L.) genes sym33 and sym40 control infection thread formation and root nodule function.

Two novel non-allelic mutants that were unable to fix nitrogen (Fix ) were obtained after EMS (ethyl methyl sulfonate) mutagenesis of pea (Pisum sativum L.). Both mutants, SGEFix(-)-1) and SGEFix(-)-2, form two types of nodules: SGEFix(-)-1 forms numerous white and some pink nodules, while mutant SGEFix(-)-2 forms white nodules with a dark pit at the distal end and also some pinkish nodules. Both mutations are monogenic and recessive. In both lines the manifestation of the mutant phenotype is associated with the root genotype. White nodules of SGEFix(-)-1 are characterised by hypertrophied infection threads and infection droplets, mass endocytosis of bacteria, abnormal morphological differentiation of bacteroids, and premature degradation of nodule symbiotic structures. The structure of the pink nodules of SGEFix(-)-1 does not differ from that of the parental line, SGE. White nodules of SGEFix(-)-2 are characterised by "locked" infection threads surrounded with abnormally thick plant cell walls. In these nodules there is no endocytosis of bacteria into host-cell cytoplasm. The pinkish nodules of SGEFix(-)-2 are characterised by virtually undifferentiated bacteroids and premature degradation of nodule tissues. Thus, the novel pea symbiotic genes, synm40 and sym33, identified after complementation analysis in SGEFix(-)-1 and SGEFix(-)-2 lines, respectively, control early nodule developmental stages connected with infection thread formation and function.

Cell Wall↗

Genetic mapping and functional analysis of a nodulation-defective mutant (sym19) of pea (Pisum sativum L.).

The pea mutant line P55 is defective in root nodule formation, and this phenotype is controlled by a single recessive gene. Complementation analysis revealed that the mutation in P55 is allelic to sym19, which has previously been mapped to linkage group I. Detailed mapping revealed that the sym19 and ENOD40 loci are separated by 2.7 cM. We identified four recombination events, demonstrating that the nodulation defect caused by mutation of the sym19 locus cannot be due to mutation of ENOD40. RT-PCR experiments showed that P55 expresses ENOD12A, but there was little or no increase in the level of its transcript in response to Nod factor or infection with Rhizobium. To investigate this expression pattern further, transgenic peas carrying a pENOD12A-GUS reporter construct were made. One transgenic line was crossed with line P55, to generate F2 progeny homozygous for sym19 and carrying pENOD12A-GUS. In both WT and sym19 mutant lines, ENOD12A-GUS expression was induced at sites of lateral root emergence in uninoculated plants. In Nod+ plants pENOD12A-GUS was induced in response to Rhizobium leguminosarumn bv. viciae, but no such induction was seen in the Nod- (sym19) mutants.

Alleles↗