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PubMed2002

Characterisation by proteomics of peribacteroid space and peribacteroid membrane preparations from pea (Pisum sativum) symbiosomes.

The legume Rhizobium symbiosis leads to the formation of a new compartment in the plant cell, the symbiosome. This compartment harbours the bacteroids surrounded by a peribacteroid membrane (PBM) originating from the plant plasma membrane. The PBM and the space between the PBM and the bacteroid membrane, called peribacteroid space (PS), mediate the exchange of metabolites between the symbionts. Proteome analysis was used as an approach to characterise the proteins in the PBM and the PS. A standard differential centrifugation procedure including a Percoll gradient was used for symbiosome isolation from pea root nodules. Proteins in the PBM and PS fractions obtained from the symbiosomes were separated by two-dimensional gel electrophoresis, and 89 spots were analysed by tandem mass spectrometry. The proteins of 46 spots could be identified by database search. The results showed that PS and even PBM preparations from pea symbiosomes always contain abundant amounts of bacteroid proteins as a contaminate. Interestingly, in addition to a few PS/PBM proteins a number of endomembrane proteins (less likely representing a contaminate), including V-ATPase, BIP, and an integral membrane protein known from COPI-coated vesicles, were found in the PBM fraction, supporting the role of the endomembrane system in PBM biogenesis.

Amino Acid Sequence↗
PubMed1992

Tissue-specific variation of pea mitochondrial polypeptides detected by computerized image analysis of two-dimensional electrophoresis gels.

A tissue-specific variation of a total of 152 mitochondria-associated polypeptides is detailed for etiolated leaves, epicotyls and roots from the pea, Pisum satisum L., using computerized image analysis. These organ systems possess, respectively, 128, 100, and 96 mitochondria-associated polypeptides with 38, 8, and 10, respectively, being unique to each. Seventy-one polypeptides were observed to be present in all gels, but some of these also underwent a variety of quantifiable changes. Two polypeptides were identified that varied similarly to a polypeptide of interest (W), known to be abundant in pea epicotyls and potato tubers. It is postulated that these latter three polypeptides are therefore probably related functionally.

Electrophoresis, Gel, Two-Dimensional↗
PubMed1987

[Quality changes in the storage of vegetable peas (Pisum sativum L.). 2. Nutritional physiologic quality].

In tests extending over several years the typical changes in the nutritional quality as occur during storage at defined temperatures (0 ... 18 degrees C) were determined in dependence on the duration of storage (chi in days). Due to the nutrient transfer from the pods to the seeds, a temporary major rise of the dry matter content (DM) is recorded in the latter together with a strongly inhibited reduction of the mono- and disaccharide content. Green peas stored without pods show a linear decrease in the DM content, degressively increasing DM losses and a more distinct reduction of saccharides. When stored with the pods, the typical decline of the vitamin C (ascorbic acid + dehydroascorbic acid) [changes in the content according to the equation y = alpha 0 + beta 1e-c theta chi and losses according to y = beta 1(1 - e-c theta chi)] goes back, mainly owing to an essentially lower coefficient for c theta. In addition, there are smaller losses in the total carotene content of such crops in the first stage of storage (losses of y = beta 1 chi 2). When storing peas without pods, we observe a a faster accumulation of the titratable total acid (up to 160%). The greatest influence on range and degree of the changes in the chemical constituents is exerted by the storage temperature. The form of the harvested crop, varietal characteristics and annual growing conditions have less bearing. Relationships and physiological causes are discussed.

Fabaceae↗
PubMed1985

Photoregulated expression of a pea rbcS gene in leaves of transgenic plants.

A 2.4-kb pea genomic fragment, containing a member (rbcS-E9) of the multigene family encoding the small subunit (rbcS) of ribulose-1,5-bisphosphate carboxylase, was inserted into a non-oncogenic, Ti-plasmid vector and introduced into the genomes of Petunia hybrida (Mitchell) and Nicotiana tabacum (SR1) plants by in vitro transformation. Petunia and tobacco plants containing the introduced pea rbcS-E9 gene were regenerated from protoplasts. In these transgenic plants the rbcS-E9 gene is transcribed accurately using its own promoter and its expression is light-induced and organ-specific. A deletion mutant with 352 bp of 5'-upstream sequence still retains photoinducibility and leaf-specific expression. Clonal analysis of independent transgenic petunia plants revealed that chromosomal positions in the recipient plant genome affect the quantitative but not qualitative aspects of rbcS-E9 expression.

Journal Article↗
PubMed1986

A sixth subunit of ATP synthase, an F(0) component, is encoded in the pea chloroplast genome.

DNA from pea and tobacco chloroplasts hybridizes specifically with probes derived from the gene for a membrane component, the a subunit of ATP synthase of the cyanobacterium, Synechococcus 6301. DNA sequence of the hybridizing region of the pea plastid DNA has revealed that it encodes a protein of 247 amino acids related in sequence to the a subunits of ATP synthase of Escherichia coli, Synechococcus and mitochondria. This is the sixth component of chloroplast ATP synthase that is plastid coded. The gene is located upstream from the genes for three other ATP synthase subunits and a transcript of 6 kb contains coding sequences from each of these genes. Thus the subunit a gene is part of a co-transcribed cluster of four ATP synthase genes arranged in the order a:c(or III):b(or I):alpha. Two other ATP synthase genes, those for beta and epsilon subunits, are known to form a separate cluster. These gene arrangements are most closely related to those found in the cyanobacterium, Synechococcus 6301. Hence, this finding provides strong evidence for a common origin for cyanobacteria and plant chloroplasts.

Journal Article↗
PubMed1993

Localization of free and bound biotin in cells from green pea leaves.

Cytosol and vacuoles from protoplasts, chloroplasts, and mitochondria from green pea (Pisum sativum) leaves were purified and examined for their biotin content. The bulk of free biotin was shown to be exclusively associated with the cytosolic fraction at a concentration of about 4 pmol/mg protein and no bound biotin was detected. The bulk of bound biotin (biotin-containing carboxylases) was associated with the soluble fraction of chloroplasts and mitochondria at a concentration of about 1.2 and 13 microM, respectively. No free biotin was detected in these organelles. Western blot analysis of total, chloroplastic, and mitochondrial polypeptides, using horseradish peroxidase-labeled streptavidin, revealed three biotin-containing polypeptides with molecular mass of 220,000, 76,000 and 34,000. All were detected in the total pea leaf extract, but the M(r) 76,000 and the M(r) 34,000 biotinylated polypeptides were only detected in mitochondria and chloroplasts, respectively. 3-Methylcrotonyl-coenzyme A carboxylase and acetyl-coenzyme A carboxylase activities were measured in these two compartments, respectively. Previously, it has been shown that the M(r) 76,000 polypeptide was the biotinylated subunit of the mitochondrial 3-methylcrotonyl-coenzyme A carboxylase. In this paper, the origin and putative function of free biotin located in cytosol are discussed.

Biotin↗
PubMed1994

Purification and N-terminal sequence analysis of pea chloroplast protein synthesis factor EF-G.

Chloroplast protein synthesis elongation factor G (chlEF-G) has been purified from whole-cell extracts of light-induced pea (Pisum sativum) seedlings. The first step in the purification scheme relies on the affinity of organellar EF-G for Escherichia coli ribosomes in the presence of the antibiotic, fusidic acid. A complex between organellar EF-G, E. coli ribosomes, GDP, and fusidic acid was isolated by high-speed centrifugation. The largest major protein eluted from this complex by high salt has an apparent molecular weight of 86,000 and is only a minor component of similar preparations from dark-grown seedlings. The same polypeptide copurifies with EF-G activity upon size exclusion HPLC on a Waters Protein-Pak 200SW column. The N-terminal amino acid sequence of chlEF-G has been determined by direct sequencing of gel-purified protein. Like many proteins that are processed upon import into chloroplasts, it has an N-terminal alanine residue. Part of the putative chlEF-G gene has been amplified using oligonucleotides corresponding to the N-terminal amino acid sequence of the purified protein and to highly conserved sequences within the GTP-binding domains of other elongation factors. The deduced amino acid sequence displays high sequence identity to the corresponding region of the chloroplast EF-G gene product from soybean, somewhat less similarity to bacterial EF-Gs, and only low homology to mitochondrial EF-G and to eukaryotic cytoplasmic EF-2 genes. The chlEF-G gene appears to be encoded by a two-copy gene family in pea and a single-copy gene in Arabidopsis thaliana.

Amino Acid Sequence↗
PubMed1999

Pea chloroplast glyceraldehyde-3-phosphate dehydrogenase has uracil glycosylase activity.

Pea (Pisum sativum) chloroplastic glyceraldehyde-3-P dehydrogenase (EC 1.2.1.13) was tested for uracil DNA glycosylase activity. It was found that both the chloroplast and the recombinant subunit B dehydrogenases remove uracil from poly(dA[3H]dU). The glycosylase activity of the recombinant subunit B enzyme and that of a truncated form corresponding in length to subunit A were associated with the dehydrogenase activity in gel-filtration experiments. Both activities of the chloroplast enzyme were inhibited by antisera raised against recombinant subunit B, and both activities of the recombinant subunit B enzyme were inhibited by antisera raised against pea chloroplast glyceraldehyde-3-P dehydrogenase. Antisera raised against Escherichia coli uracil glycosylase did not affect the glycosylase activity of the recombinant subunit B enzyme. The glycosylase pH activity profile of the chloroplast dehydrogenase was unique. It is distinct from the dehydrogenase pH activity profile and from the pH activity profiles of other plant glycosylases. The glycosylase activity, but not the dehydrogenase activity, of the recombinant subunit B enzyme was inhibited by uracil. Pyridine nucleotides stimulated the glycosylase activity. To our knowledge this is the first example of a nonhuman glyceraldehyde-3-P dehydrogenase, and of an NADP-dependent glyceraldehyde-3-P dehydrogenase, that exhibits uracil glycosylase activity.

Amino Acid Sequence↗
PubMed2000

Characterization of two novel defense peptides from pea (Pisum sativum) seeds.

A fraction that possesses antifungal activity against Aspergillus niger has been isolated from seeds of the pea (Pisum sativum) by ammonium sulfate fractionation followed by gel filtration on Sephadex G-75. On further purification by reverse-phase high performance liquid chromatography, two small cysteine-rich polypeptides were obtained (Psd1 and Psd2). They are localized primarily in vascular bundles and epidermis tissues of pea pods and exhibit high antifungal activity toward several fungi, displaying IC(50) values ranging from 0.04 to 22 microg/ml. This inhibitory activity decreases when A. niger growth medium is supplemented with cations such as Ca(2+), Mg(2+), Na(+), and K(+). Although the primary sequence of both Psd1 and Psd2 shows homology with other plant defensins, they cannot easily be assigned to any established group.

Amino Acid Sequence↗
PubMed1995

Calreticulin is the major Ca2+ storage protein in the endoplasmic reticulum of the pea plant (Pisum sativum).

A 56kDa protein with high similarity in its N-terminal amino acid sequence to animal calreticulin and 100% homology with the N-terminal amino acids of spinach calreticulin has been identified in seeds of the pea plant (Pisum sativum). A new purification procedure is described by which the calreticulin-like protein was selectively solubilized by incubation with deoxycholate and HgCl2 from microsomes enriched for endoplasmic reticulum. Following Mono Q ion exchange chromatography of the deoxycholate extract by fast protein liquid chromatography, the calreticulin-like protein was obtained in nearly pure form. This purified protein is similar to animal calreticulin in apparent mass, characteristic blue staining with Stains-all dye and calcium-binding ability. In addition, this protein is recognized only by affinity purified antibodies against rabbit calreticulin and is not recognized by anti-calsequestrin antibodies. Our data suggested that calreticulin rather than calsequestrin functions as the Ca(2+)-storage protein in the endoplasmic reticulum of pea plants.

Amino Acid Sequence↗
PubMed1998

Inhibition of pea chloroplast DNA helicase unwinding and ATPase activities by DNA-interacting ligands.

DNA helicases unwind the duplex DNA in an ATP dependent manner and thus play an essential role in DNA replication, repair, recombination and transcription. Any DNA-interacting ligand which will modulate DNA helicase activity may interrupt practically all kinds of DNA transactions. There are no studies on the effect of various cytotoxic DNA-interacting ligands on organelle helicases. We have determined the effect of camptothecin, VP-16 (etoposide), ellipticine, genistein, novobiocin, m-AMSA, actinomycin C1, ethidium bromide, daunorubicin and nogalamycin on unwinding and ATPase activities of purified chloroplast DNA helicase from pea (Pisum sativum). Our study has shown that DNA-intercalating ligands actinomycin C1, ethidium bromide, daunorubicin and nogalamycin were inhibiting the DNA unwinding activity with an apparent Ki of 2.9 microM, 3.0 microM, 1.4 microM and 1.0 microM, respectively. These four inhibitors also inhibited the ATPase activity of pea chloroplast DNA helicase. These results indicate that the intercalation of the inhibitors into DNA generates a complex that impedes the translocation of chloroplast DNA helicase, resulting in both inhibition of unwinding activity and ATP hydrolysis. This study would be useful for understanding the mechanism of organelle DNA helicase unwinding and the mechanism by which these DNA-interacting ligands inhibit cellular function.

Adenosine Triphosphatases↗
PubMed2002

Detoxication mechanism of exogenous monatomic phenols in pea seedlings.

The conversion of exogenous monatomic phenols (O-[1-(14)C]nitrophenol, 2,4-[1-14C]dinitrophenol, and alpha-[1-14C]naphthol) in pea seedlings has been investigated. It has been found that in the pea seedlings glycosylation of these phenols does not occur, but the main pathway of their detoxication is conjugation with the low-molecular-weight peptides. Approximately 80% of phenols absorbed by seedlings form phenol-peptide conjugates. The part of exogenous monatomic phenols is irreversibly bound to proteins via quinone-protein interaction. The amino acid content of the peptides involved in the conjugation process has been established. Penetration into the plant of monatomic exogenous phenols with a high dissociation constant leads to the stimulation of peptide formation.

2,4-Dinitrophenol↗
PubMed1998

The laboratory preference of annual legumes by pea weevil sitona lineatus L. (Col., curculionidae) and their effect on susceptibility of weevils to entomogenous nematodes.

The activity and natural mortality of Sitona lineatus weevils during the egg laying period may be connected with host plant preference. Preference of S. lineatus adults for early field pea and other pea cultivars influences their low feeding activity and results in lopff average body weight and higher susceptibility to entomogenous nematodes, Steinernema carpocapsae, S. feltiae, and Heterorhabditis bacteriophora.

Animals↗
PubMed1995

Transcriptional regulation of PS-IAA4/5 and PS-IAA6 early gene expression by indoleacetic acid and protein synthesis inhibitors in pea (Pisum sativum).

The transcription of two genes, PS-IAA4/5 and PS-IAA6, in pea is induced by indoleacetic acid (IAA) and protein synthesis inhibitors such as cycloheximide (CHX) and anisomycin (ANI). Induction by IAA is rapid, taking 5 and 7.5 minutes for PS-IAA4/5 and PS-IAA6, respectively, and is independent of IAA concentration and whether IAA has a free or esterified carboxyl group (ethyl-IAA). The rate of mRNA accumulation, however, is dependent on hormone concentration, and is greater with IAA than with ethyl-IAA. The turnover rates (t1/2) of the PS-IAA4/5 and PS-IAA6 mRNAs are 60 and 75 minutes, respectively, and are not affected by IAA. CHX or ANI induce the transcription of PS-IAA4/5 and PS-IAA6 more slowly than IAA (5 to 10 minutes for PS-IAA4/5 and 20 minutes for PS-IAA6). While protein synthesis inhibitors stabilize both mRNAs, the rapidity of induction by CHX and ANI cannot be accounted for solely by mRNA stabilization. The relationship between mRNA induction and protein synthesis inhibition does not obey Michaelis-Menten kinetics, but rather is best described by a hyperbolic curve, suggesting the release of transcriptional repression by the inhibition of protein synthesis. RNA expression experiments with transgenic tobacco seedlings or with transfected pea protoplasts using PS-IAA4/5 promoter GUS or CAT fusions reveal that CHX transcriptionally activates PS-IAA4/5 gene expression. Thus, protein synthesis inhibitors have a dual effect on PS-IAA4/5 and PS-IAA6. (1) They stabilize both mRNAs (possibly by a translational arrest-linked process or by preventing the synthesis of a labile nuclease(s)). (2) They activate transcription (possibly by preventing the synthesis or function of a repressor).

Anisomycin↗
PubMed1999

Purification and characterization of amine oxidase from pea seedlings.

A novel, simple, and rapid procedure for the purification of pea seedling amine oxidase is reported. The crude enzyme, obtained by ammonium sulfate fractionation, was purified in two steps: the first one by anion-exchange chromatography and the second one by affinity chromatography. The first chromatography step was carried out on a diethylaminoethyl-cellulose column. By lowering the amount of protein loaded on the column and the buffer concentration it was possible to obtain an enzyme pure at 95% (sp act 1.2 microkat/mg). To achieve a higher degree of purification various affinity resins were prepared and tested. The resins were obtained by covalent immobilization of polyamines on Sepharose according to three different procedures. The best results were obtained with 6-aminohexyl-Sepharose 2B, prepared using CNBr as coupling agent, and eluting the enzyme by a solution containing 1, 4-diaminocyclohexane. This last compound was found to be a relatively strong competitive inhibitor of the oxidative deamination of cadaverine catalyzed by pea seedling amine oxidase (Ki = 32 microM). According to this procedure an electrophoretically homogeneous enzyme, characterized by a specific activity of 1.63 microkat/mg, was obtained.

Amine Oxidase (Copper-Containing)↗
PubMed1983

Intoxication by the chickling pea (Lathyrus sativus): nervous system and skeletal findings.

Two hundred patients with chronic neurolathyrism were examined 25-35 years after the appearance of signs and symptoms of intoxication of the chickling pea. Their daily food intake, in a German forced labor camp during World War II, consisted of 400 g Lathyrus sativus peas cooked in water plus 200 g bread baked of barley and straw. Apart from the classic signs of neurolathyrism, i.e., a spastic paraparesis, in five cases, the skeletal findings observed were similar to experimental osteolathyrism. There was an absence of ossification centers of the iliac creasts, ischial tuberosities and vertebrae; and bowing with thickening of the femoral shaft also occurred. These bony changes in human lathyrism have not been described before.

Adolescent↗
PubMed1993

The importance of starch biosynthesis in the wrinkled seed shape character of peas studied by Mendel.

The wrinkled-seed mutant (rr) of pea (Pisum sativum L.) arose through mutation of the gene encoding starch-branching enzyme isoform I (SBE1) by insertion of a transposon-like element into the coding sequence. Two isoforms of starch-branching enzyme have been documented in the developing pea embryo. The second isoform, SBEII, is expressed towards the later stages of embryo development while SBEI is expressed highly in the early stages. Due to mutation of SBEI the total amount of starch and the proportion of amylopectin, a branched starch polymer, are greatly reduced in the wrinkled (rr) line as compared to that in the wild-type, round (RR) line. Consequently, the level of sucrose in the rr line is nearly two fold that of the RR line. Increased sucrose concentration in the developing embryos of this mutant line causes increased uptake of water and thereby increases the cell size and fresh weight. During seed maturation in these mutant seeds a greater loss of water occurs. As a result, the wrinkled seed phenotype develops. Besides this morphological variation, the mutation also causes changes in the amount of lipid and of one storage protein, legumin. This review article discusses the role of the SBEI enzyme in causing such metabolic changes in the developing embryos with the implication that metabolism can play a central role in plant development.

1,4-alpha-Glucan Branching Enzyme↗
PubMed1995

Sequential induction of the ethylene biosynthetic enzymes by indole-3-acetic acid in etiolated peas.

Ethylene induced an increase in the accumulation of 1-aminocyclopropane-1-carboxylate (ACC) oxidase transcript level and enzyme activity in the first internode of 5- to 6-day-old etiolated pea (Pisum sativum L.) seedlings. Indole-3-acetic acid (IAA), which stimulates ethylene production by enhancing ACC synthase activity, also caused an increase in ACC oxidase transcript and activity levels. The IAA-induced increase in ACC oxidase mRNA level and enzyme activity was blocked by 2,5-norbornadiene (NBD), a competitive inhibitor of ethylene action. This indicates that IAA induced ACC oxidase through the action of ethylene. The level of ACC synthase mRNA and enzyme activity started to increase less than 1 h after the start of IAA treatment, whereas ACC oxidase activity and transcript levels began to rise after 2 h of IAA treatment. These results indicate that the enzymes of ethylene biosynthesis are sequentially induced after treatment of intact pea seedlings with IAA. The increase in ACC synthase activity leads to the production of ACC, which is converted by the low constitutive level of ACC oxidase activity to ethylene. Through a positive feedback loop, ethylene promotes the accumulation of ACC oxidase mRNA and the increase in ACC oxidase activity.

Amino Acid Oxidoreductases↗