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PubMed1980

The amino acid sequence of pea (Pisum sativum) leghemoglobin.

The amino acid sequence has been determined for leghemoglobin component I from root nodules of pea, Pisum sativum. Pea leghemoglobin is one polypeptide chain composed of 147 amino acids, it contains one methionine residue at position 144, and three histidines, which are at positions 60, 92 and 101. The sequence has at least seven polymorphic residues, but it was not possible to separate the polymorphic protein forms which had identical electric charge. The approximate molecular weight of pea leghemoglobin component I is 16,350. The other major leghemoglobin component (II) from pea has an amino acid composition very similar to that of leghemoglobin component I, suggesting that the gene has duplicated relatively recently. P. sativum leghemoglobin differs from that of Vicia faba by 22--23%, depending on the polymorphic form. The leghemoglobins from Phaseolus vulgaris and Glycine max differ from pea leghemoglobin by 35--44%, and Lupinus luteus leghemoglobins differ from it by 45--48%. The seven leghemoglobins so far sequenced have 50 residues (33%) which are common to all.

Amino Acid Sequence↗

PubMed1987

[13N]-beta-phenethylamine ([13N]PEA): a prototype tracer for measurement of MAO-B activity in heart.

[13N]beta-Phenethylamine ([13N]PEA) was evaluated as a radio tracer for the measurement of mouse heart monoamine oxidase (MAO) activity in vivo. After intravenous administration, [13N]PEA was deaminated by MAO-B. 13NH3 formed thereby was taken up by amino acids and trapped in the heart. The relation between the radioactivity trapped in the heart and the enzyme activity was examined. The radioactivity in the heart 15 min after administration was reduced in a dose-dependent manner by pretreatment with a specific MAO-B inhibitor, l-deprenyl, but not with a specific MAO-A inhibitor, clorgyline. A linear correlation existed between the heart radioactivity level and the heart MAO-B activity (0-45%). [13N]1,1-d2-2-Phenethylamine (C6H5-CH2-CD2-13NH2, [13N]d2PEA), a modified tracer with less reactivity towards the enzyme, was tested similarly. This tracer possessed a higher sensitivity than [13N]PEA, and a wider range (0-85%) of MAO-B activity correlated linearly with the trapped radioactivity. These results indicate that [13N]PEA derivatives ([13N]PEA and [13N]d2PEA) can be useful radiotracers for noninvasive measurements of MAO-B activity in the human heart.

Ammonia↗

PubMed1995

Metabolism of xyloglucan generates xylose-deficient oligosaccharide subunits of this polysaccharide in etiolated peas.

Oligosaccharide subunits of xyloglucan were isolated from the stems and roots of etiolated pea plants and structurally characterized. The two most abundant subunits of pea xyloglucan are the well-known nonasaccharide, XXFG, and heptasaccharide, XXXG. In addition, significant amounts of oligosaccharides that have not previously been reported to be subunits of pea xyloglucan were detected, including a decasaccharide, XLFG, two octasaccharides, XLXG and XXLG, a pentasaccharide, XXG, and a trisaccharide, XG. Several novel oligosaccharide subunits, including the octasaccharide, GXFG, and the hexasaccharide, GXXG, were also found. Xyloglucan oligosaccharides generated by treatment of intact pea stem cell walls were compared to oligosaccharides generated by endoglucanase treatment of xyloglucan polysaccharides obtained by subsequent alkali extraction of the same cell walls. The results suggest that the xyloglucan in etiolated pea stems is distributed between at least two domains, one of which is distinguished by its enzyme accessibility. We further hypothesize that the chemical modification of a xyloglucan during cell-wall maturation depends on its physical environment (i.e., the domain in which it resides). For example, only the endoglucanase-released material, representing the enzyme-accessible xyloglucan domain, contains significant amounts of the two unusual oligosaccharide subunits, GXXG and GXFG, both of which have a nonreducing terminal glucosyl residue. This structure may be generated during cell-wall maturation by the sequential action of an endolytic enzyme (such as xyloglucan endotransglycosylase or endoglucanase) and an alpha-xylosidase.

Carbohydrate Sequence↗

PubMed1975

The isolation of allergens from the green pea.

The aqueous extract of green peas was separated into 3 fractions (albumin, legumin, and vicilin) by dialysis against distilled water and isoelectric precipitation. The major antigenic and all of the allergenic activity of the pea extract was associated with the albumin fraction. The albumin fraction retains its allergenicity upon heating at 60 degrees C for 30 min or boiling at 100 degrees C for 5 min, but becomes partially inactivated by autoclaving at 120 degrees C for 15 min. The allergenic determinant expressed by the albumin fraction appears to be common to several other members of the legume family. In addition, the pea dialysate fraction was shown to specifically inhibit precipitin and passive cutaneous anaphylaxis (PCA) reactions involving rabbit antipea serum and the pea albumin fraction, and histamine release from passively sensitized monkey lung tissue using the serum of pea-sensitive patients.

Albumins↗

PubMed1991

Distribution of type I phytochrome (phyA) RNA1 and RNA2 in etiolated pea seedlings.

Four-day-old etiolated pea seedlings were divided into 11 parts along the axis, from which poly(A)+ RNA and DNA were extracted. Using a slot-blot hybridization assay, the abundance of pea type I phytochrome (phyA) poly(A)+ RNA was measured in each portion of the etiolated pea seedling. For the quantification of the phyA RNA, pea phyA RNA synthesized in vitro was used as an RNA standard. The hook region contained the highest abundance of phyA RNA (approximately 0.3 ng phyA RNA per microgram DNA) in the etiolated seedling. Two mRNAs of different length (the shorter designated as RNA1 and the longer RNA2) are produced in detectable amounts from single pea phyA in the etiolated seedling; the ratio of the abundance of phyA RNA1 to phyA RNA2 was determined in each of the 11 parts by a primer extension assay. The abundance of phyA RNA1 in the plumule and hook regions was 3-5-fold higher than that of RNA2, whereas the ratio of their abundance was approximately unity in other regions. A time course study of the abundance of both RNAs was carried out during the imbibition of seeds and indicated that the accumulation of phyA RNA1 occurred more rapidly in the cotyledons than that of RNA2 during the first day of imbibition, whereas the accumulation of phyA RNA2 increased rapidly during the second day and became as high as that of phyA RNA1 by the third day.

Base Sequence↗

PubMed2006

Evaluation of fluoranthene phytotoxicity in pea plants by Hill reaction and chlorophyll fluorescence.

The effect of both increased concentrations (0.01 and 1 mg l(-1)) of fluoranthene (FLT) and the duration of exposure (18 and 25 days) on the growth and photosynthetic processes in pea plants (Pisum sativum L., cv. Garde) was investigated. FLT concentration in roots and shoot of pea plants was also determined. The obtained results demonstrated that the higher concentration of FLT (1 mg l(-1)) significantly inhibited the growth of the pea plants after 25 days of the application, also affected the content of photosynthetic pigments (chlorophyll a, b and carotenoids), and the primary photochemical processes of photosynthesis. In chlorophyll fluorescence parameters, the significant increase of F(0) values and the decrease of F(V)/F(M) and Phi(II) values was recorded. The Hill reaction of isolated chloroplasts of pea plants was significantly inhibited after 25 days by presence of FLT (0.01 and 1 mg l(-1)) in nutrient solution, while after 18 days no significant response of Hill reaction activity was recorded. The fluoranthene content in roots and shoot of pea plants increased with increasing FLT concentration in the environment and the substantial accumulation of FLT was observed in the roots.

Biomass↗

PubMed2003

The multifunctional protein PEA-15 is involved in the control of apoptosis and cell cycle in astrocytes.

PEA-15 is a small protein (15 kDa) that was first identified as an abundant phosphoprotein in brain astrocytes [Araujo et al., J Biol Chem 1993;268(8):5911-20], and subsequently shown to be widely expressed in different tissues and highly conserved among mammals [Estelles et al., J Biol Chem 1996;271(25):14800-6; Danziger et al., J Neurochem 1995;64(3):1016-25]. It is composed of a N-terminal death effector domain and a C-terminal tail of irregular structure. PEA-15 is regulated by multiple calcium-dependent phosphorylation pathways that account for its different forms: a non-phosphorylated form in equilibrium with a mono and a biphosphorylated variety. This already suggested that PEA-15 may play a major role in signal integration. Accordingly, it has been demonstrated to modulate signaling pathways that control apoptosis and cell proliferation. In particular, PEA-15 diverts astrocytes from TNFalpha-triggered apoptosis and regulates the actions of the ERK MAP kinase cascade by binding to ERK and altering its subcellular localization. The three-dimensional structure of PEA-15 has been modelized and recently determined using NMR spectroscopy, and may help to understand the various functions played by the protein through its molecular interactions.

Animals↗

PubMed1999

Cloning and characterisation of a pea mitochondrial NDPK.

Here we report the cloning of a cDNA encoding the first nucleoside diphosphate kinase (NDPK) isolated from plant mitochondria. Amplification of a 317 nt product was performed by PCR, using oligonucleotide primers based on partial amino acid sequences of the pea mitochondria NDPK and other NDPK isoforms. By screening of a pea cDNA library with this PCR product, a full length clone was obtained. Northern analysis revealed the presence of a 1.1 kb single transcript, with high expression in young leaves and reproductive tissues. The clone encodes a precursor protein of 232 amino acids (26 kDa), including an N-terminal extension of 80 amino acids (9 kDa). Analysis of the deduced amino acid sequence confirmed its identity with the sequences obtained from the purified mature pea mitochondrial NDPK. In vitro import experiments carried out in isolated pea mitochondria showed targeting and processing of the 27 kDa precursor into a 16.5 kDa mature form. Phylogenetic analysis of some vertebrate and plant isoforms of NDPK showed that the pea mtNDPK groups together with the NDPK3 isoform from A. thaliana and the chloroplastic NDPK III from spinach. We suggest that it is possible to design a novel classification of the different NDPK isoforms according to their subcellular localisation and origin.

Amino Acid Sequence↗

PubMed2001

Cloning and expression of a nuclear encoded plastid specific 33 kDa ribonucleoprotein gene (33RNP) from pea that is light stimulated.

We report the cloning and sequencing of both cDNA and genomic DNA of a 33 kDa chloroplast ribonucleoprotein (33RNP) from pea. The analysis of the predicted amino acid sequence of the cDNA clone revealed that the encoded protein contains two RNA binding domains, including the conserved consensus ribonucleoprotein sequences CS-RNP1 and CS-RNP2, on the C-terminus half and the presence of a putative transit peptide sequence in the N-terminus region. The phylogenetic and multiple sequence alignment analysis of pea chloroplast RNP along with RNPs reported from the other plant sources revealed that the pea 33RNP is very closely related to Nicotiana sylvestris 31RNP and 28RNP and also to 31RNP and 28RNP of Arabidopsis and spinach, respectively. The pea 33RNP was expressed in Escherichia coli and purified to homogeneity. The in vitro import of precursor protein into chloroplasts confirmed that the N-terminus putative transit peptide is a bona fide transit peptide and 33RNP is localized in the chloroplast. The nucleic acid-binding properties of the recombinant protein, as revealed by South-Western analysis, showed that 33RNP has higher binding affinity for poly (U) and oligo dT than for ssDNA and dsDNA. The steady state transcript level was higher in leaves than in roots and the expression of this gene is light stimulated. Sequence analysis of the genomic clone revealed that the gene contains four exons and three introns. We have also isolated and analyzed the 5' flanking region of the pea 33RNP gene.

Amino Acid Sequence↗

PubMed1998

PPF-1, a post-floral-specific gene expressed in short-day-grown G2 pea, may be important for its never-senescing phenotype.

We cloned a developmentally regulated gene from a cDNA library constructed from short-day (SD) grown G2 pea tissue using cDNA representational difference analysis (cDNA RDA) and named it PPF-1 for the first Pisum sativum post-floral-specific gene. Sequence comparisons with various databases revealed that PPF-1 shares a substantial homology only at the deduced amino-acid level with the Bacillus subtilis gene SP3J, which is required for maintaining vegetative growth, and with other genes coding for bacterial inner membrane proteins. All five potential hydrophobic regions from the bacterial proteins were maintained in the PPF-1 sequence. A series of Northern blots showed that this gene was only expressed after floral initiation and was limited to the apical buds, with non-detectable levels in roots, stems and mature leaves. Under SD conditions, when G2 pea displays an unlimited growth habit, PPF-1 expression was sustained at a relatively high level long after floral initiation. Under long-day (LD) conditions, when G2 pea undergoes an apical senescence similar to wild-type plants with genotype sn hr, PPF-1 was only expressed very briefly after flower initiation. Interestingly, in day-neutral, wild-type Alaska pea, the PPF-1 level was hardly detectable under any growth conditions. Treatment of LD-grown G2 pea with gibberellin A3 (GA3) was able to stimulate PPF-1 expression unless it was applied at a very late growth stage, at which time the process of apical senescence cannot be reversed.

Amino Acid Sequence↗

PubMed1999

Transcriptional activation of the parsley chalcone synthase promoter in heterologous pea and yeast systems.

Introduction by electroporation of different parsley (Petroselinum crispum) CHS-promoter/beta-glucuronidase(GUS)-reporter constructs into pea (Pisum sativum L.) protoplasts leads to a high constitutive GUS-expression and to the loss of the light-inducibility seen in the homologous parsley protoplast system. These results indicate that Unit 1 of the parsley CHS-promoter is only partly responsible for the GUS-expression detected. Instead, additional cis-elements, which are located downstream within 100 bp from the transcriptional start site, mediate the de-repression in pea protoplasts. In contrast, in yeast (Saccharomyces cerevisiae) cells, the GUS expression from the heterologous CHS/GUS construct is controlled by elements between Unit 1 and -100 bp. In both pea and yeast cells, transcription factors different from those regulating UV-responsiveness in parsley, are probably mediating the constitutive expression from the heterologous construct. The results with pea protoplasts imply that protoplastation of pea leaf cells itself induces de-repression as a result of stress to the protoplasts. This notion was strengthened by the finding that mRNA levels of the endogenous chalcone synthase were drastically increased as the result of the protoplastation procedure.

Journal Article↗

PubMed2005

Influence of maturation on the alteration of allergenicity of green pea (Pisum sativum L.).

The IgE-binding capacity of different maturation levels of green pea seeds (Pisum sativum L.) of the variety Maxigolt is examined to determine the influence of maturation on the alteration of allergenicity. Different protein extraction methods to get total protein extracts and the protein fractions glutelin, globulin, and albumin from different maturation levels of green pea seeds are applied to SDS-PAGE/silver staining as well as SDS-PAGE/immunoblotting and EAST inhibition experiments using sera of 15 green pea allergic individuals. The SDS-PAGE/silver-staining experiments show the continuous change of protein pattern during maturation. SDS-PAGE/immunoblot and EAST inhibition demonstrate that all levels of green pea seeds show relevant IgE-binding capacity, as do immature seeds. Total IgE-binding capacity rises with the progress of maturation. Although the main allergenic activity is dependent upon the albumin fraction, the glutelin and globulin fractions are also important. The implication of these results is an obvious allergenic potency of all maturation levels, even immature seeds, whereas an increase of allergenicity during maturation could be notched up. The highest allergenic potency is caused by the albumin fraction, but globulin and glutelin fractions also contribute to the allergenicity of green pea.

Adult↗

PubMed1997

The single-copy gene encoding high-mobility-group protein HMG-I/Y from pea contains a single intron and is expressed in all organs.

The coding and 3'-downstream regions of the gene encoding the high mobility group protein HMG-I/Y from pea have been isolated, sequenced and characterised. A 795 bp pea genomic fragment containing the coding region of the pea HMG-I/Y gene with a single intron of 201 bp was isolated by PCR. The gene encodes a protein of 197 amino acid residues with four copies of the AT-hook DNA-binding motif encoded by exon 2. Southern blot analysis on genomic DNA revealed the presence of a single copy of the HMG-I/Y gene in the haploid genome. The pea HMG-I/Y gene is expressed in all organs of pea including roots, stems, leaves, flowers, tendrils and developing seeds, as determined by northern blot analysis.

Amino Acid Sequence↗

PubMed2002

Specificity of auxin regulation of gibberellin 20-oxidase gene expression in pea pericarp.

During early pea fruit growth, the physiological roles of 4-chloroindole-3-acetic acid (4-Cl-IAA) and IAA, natural pea auxins, in regulating gibberellin (GA) 20-oxidase gene expression (PsGA20ox1) were tested with 4-position, ring-substituted auxins that have a range of biological activities (fruit growth). The effect of seeds, and natural and synthetic auxins (4-Cl-IAA, and IAA; 4-Me-IAA, 4-Et-IAA and 4-F-IAA, respectively), and auxin concentration (4-Cl-IAA) on PsGA20ox1 mRNA levels in pea pericarp were investigated over a 24 h treatment period. The ability of the 4-substituted auxins to increase PsGA20ox1 mRNA levels in deseeded pericarp was correlated with their ability to stimulate pericarp growth. The greatest increase in pericarp PsGA20ox1 mRNA levels and growth was observed when deseeded pericarps were treated with the naturally occurring pea auxin, 4-Cl-IAA; however, IAA was not effective. Silver thiosulfate, an ethylene action antagonist, did not reverse IAA's lack of stimulation of PsGA20ox1 over the control treatment. 4-Me-IAA was the second most active auxin in stimulating PsGA20ox1 and was the second most biologically active auxin. Application of the 4-substituted IAA analogs, 4-Et-IAA and 4-F-IAA, to deseeded pericarps resulted in minimal or no increase in PsGA20ox1 transcript levels or pericarp growth. Pericarp PsGA20ox1 mRNA levels increased with increasing 4-Cl-IAA concentration and showed transitory increases at low 4-Cl-IAA treatments (30 to 300 pmol). These results support a unique physiological role for the auxin 4-Cl-IAA in the regulation of GA metabolism by effecting PsGA20ox1 expression during early pea fruit growth.

Blotting, Northern↗

PubMed2002

Changes in phytates and HCl extractability of calcium, phosphorus, and iron of soaked, dehulled, cooked, and sprouted pigeon pea cultivar (UPAS-120).

UPAS-120, a high yielding and early maturing variety of pigeon peas released by the Department of Plant Breeding, CCS Haryana Agricultural University, Hisar contained a significant amount of phytic acid, i.e. 886 mg/100 g. When it was subjected to various domestic processing and cooking methods viz. soaking (6, 12, 18 h), dehulling, ordinary as well as pressure cooking and germination (24, 36 and 48 h), a drastic decrease in level of phytic acid with a remarkable increase in the HCl-extractability of mono, divalent, and trivalent ions, like calcium, phosphorus, and iron occurred. Germination (48 h) was found to be the best method for decreasing the phytic acid content, i.e. 35 to 39 percent less than the control and significantly (p < 0.05) increasing the non-phytate phosphorus and HCl-extractable phosphorus. Pressure cooking of soaked-dehulled pigeon pea also rendered equally good results. The calcium, phosphorus, and iron contents of pigeon pea seeds were 197.3, 473.1, and 9.91 mg/100 g, respectively; some losses varying from 3 to 9 percent were noticed when the legume was subjected to soaking, cooking, and germination but the maximum losses, i.e. 23 percent, occurred when the seeds were dehulled. However, HCl-extractability of Ca, P, and Fe improved to a significant extent when the pigeon pea seeds were soaked, soaked-dehulled, cooked and sprouted which may have been due to decrease in the phytate content followed by processing and cooking. The significant negative correlations between the phytic acid and HCl-extractability of minerals of processed pigeon pea strengthens these findings.

Biological Availability↗

PubMed2005

Structure of allelic variants of subtype 5 of histone H1 in pea Pisum sativum L.

The pea genome contains seven histone H1 genes encoding different subtypes. Previously, the DNA sequence of only one gene, His1, coding for the subtype H1-1, had been identified. We isolated a histone H1 allele from a pea genomic DNA library. Data from the electrophoretic mobility of the pea H1 subtypes and their N-bromosuccinimide cleavage products indicated that the newly isolated gene corresponded to the H1-5 subtype encoded by His5. We confirmed this result by sequencing the gene from three pea lines with H1-5 allelic variants of altered electrophoretic mobility. The allele of the slow H1-5 variant differed from the standard allele by a nucleotide substitution that caused the replacement of the positively charged lysine with asparagine in the DNA-interacting domain of the histone molecule. A temperature-related occurrence had previously been demonstrated for this H1-5 variant in a study on a worldwide collection of pea germplasm. The variant tended to occur at higher frequencies in geographic regions with a cold climate. The fast allelic variant of H1-5 displayed a deletion resulting in the loss of a duplicated pentapeptide in the C-terminal domain.

Alleles↗

PubMed1996

Effect of substituent on the thermodynamics of D-glucopyranoside binding to concanavalin A, pea (Pisum sativum) lectin and lentil (Lens culinaris) lectin.

Titration calorimetry measurements of the binding of phenyl-alpha (alpha PhOGlu), 3-methoxy (3MeOGlu), fluorodeoxy and deoxy derivatives of alpha-D-glucopyranose (Glu) to concanavalin A (conA), pea lectin and lentil lectin were performed at approx. 10 and 25 degrees C in 0.01 M dimethylglutaric acid/NaOH buffer, pH 6.9, containing 0.15 M NaCl and Mn2+ and Ca2+ ions. Apparently the 3-deoxy, 4-deoxy and 6-deoxy as well as the 4-fluorodeoxy and 6-fluorodeoxy derivatives of Glu do not bind to the lectins because no heat release was observed on the addition of aliquots of solutions of these derivatives to the lectin solutions. The binding enthalpies, delta H0b, and entropies, delta S0b, determined from the measurements were compared with the same thermodynamic binding parameters for Glu, D-mannopyranoside and methyl-alpha- D-glucopyranoside (alpha MeOGlu). The binding reactions are enthalpically driven with little change in the heat capacity on binding, and exhibit enthalpy-entropy compensation. Differences between the thermodynamic binding parameters can be rationalized in terms of the interactions apparent in the known crystal structures of the methyl-alpha-D-mannopyranoside-conA [Derewenda, Yariv, Helliwell, Kalb (Gilboa), Dodson, Papiz, Wan and Campbell (1989) EMBO J. 8, 2189-2193] and pea lectin-trimanno-pyranoside [Rini, Hardman, Einspahr, Suddath and Carber (1993) J. Biol. Chem. 268, 10126-10132] complexes. Increases in the entropy change on binding are observed for alpha MeOGlu binding to pea and lentil lectin, for alpha PhOGlu binding to conA and pea lectin, and for 3MeOGlu binding to pea lectin relative to the entropy change for Glu binding, and imply that the phenoxy and methoxy substituents provide additional hydrophobic interactions in the complex. Increases in the binding enthalpy relative to that of Glu are observed for deoxy and fluoro derivatives in the C-1 and C-2 positions and imply that these substituents weaken the interaction with the surrounding water, thereby strengthening the interaction with the binding site.

Binding Sites↗

PubMed1995

Starch branching enzymes belonging to distinct enzyme families are differentially expressed during pea embryo development.

cDNA clones for two isoforms of starch branching enzyme (SBEI and SBEII) have been isolated from pea embryos and sequenced. The deduced amino acid sequences of pea SBEI and SBEII are closely related to starch branching enzymes of maize, rice, potato and cassava and a number of glycogen branching enzymes from yeast, mammals and several prokaryotic species. In comparison with SBEI, the deduced amino acid sequence of SBEII lacks a flexible domain at the N-terminus of the mature protein. This domain is also present in maize SBEII and rice SBEIII and resembles one previously reported for pea granule-bound starch synthase II (GBSSII). However, in each case it is missing from the other isoform of SBE from the same species. On the basis of this structural feature (which exists in some isoforms from both monocots and dicots) and other differences in sequence, SBEs from plants may be divided into two distinct enzyme families. There is strong evidence from our own and other work that the amylopectin products of the enzymes from these two families are qualitatively different. Pea SBEI and SBEII are differentially expressed during embryo development. SBEI is relatively highly expressed in young embryos whilst maximum expression of SBEII occurs in older embryos. The differential expression of isoforms which have distinct catalytic properties means that the contribution of each SBE isoform to starch biosynthesis changes during embryo development. Qualitative measurement of amylopectin from developing and maturing embryos confirms that the nature of amylopectin changes during pea embryo development and that this correlates with the differential expression of SBE isoforms.

1,4-alpha-Glucan Branching Enzyme↗