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[Digestion of pea and soya proteins in the preruminant calf. II. Apparent digestibility at the end of the ileum and the digestive tube].

Three milk substitutes (control, pea and soya-bean) were given to 6 preruminant calves fitted with re-entrant canulas in the terminal ileum. In the control diet, protein was almost entirely provided by skim milk powder. In the pea diet, a pregelatinized dehulled pea flour provided 33.5% of the protein, the remainder being supplied by skim milk powder. In the soya-bean powder diet 73.2% of the protein were provided by a soya-bean isolate and the remainder by whey powder. The apparent digestibility of total nitrogen was significantly lower with the pea and soya-bean diets. than with the control diet (0.92, 0.91 and 0.95 at the end of the ileum, 0.92, 0.94 and 0.97 at the end of the whole digestive tract, respectively). Also the ileal digestibility of most amino acids decreased with the pea and soya-bean diets; the differences were greatest for cystine (-0.6; non significant) with the pea diet and for threonine (-0.7; P less than 0.01) with the soya-bean diet. Irrespective of the diet the protein escaping digestion in the small intestine appeared to be mainly from endogenous and bacterial origin. Although small amounts of partially degraded dietary protein could be present in ileal digesta with the pea and soya-bean diets, their true digestibility was probably very high.

Amino Acids↗

Enzymatic properties of the lipoxygenase from pea seeds.

A lipoxygenase preparation was obtained from dried green pea seeds. Disc electrophoresis with enzyme staining indicated the presence of only one main isoenzyme corresponding to the isoenzyme PL I according to Yoon and Klein (J. Agric. Food Chem. 24, 955 (1979)), whereas PL II was absent. The assay for pea lipoxygenase has been optimized by using a final concentration of 0.53 mM potassium linoleate in the presence or absence of 0.2% sodium cholate. Without detergent the rho H optimum was 5.9, in its presence 6.8. The formation of conjugated dienes absorbing at 234 nm accounted for 75% of the oxygen uptake. The difference is mainly due to the aerobic formation of oxodienoic acids absorbing at 285 nm via a lipohydroperoxidase activity concomitant with the dioxygenase reaction. Other lipohydroperoxidase products were formed only to a minor extent under aerobic conditions, whereas in the anaerobic lipohydroperoxidase reaction of pea lipoxygenase in the system 13L8-hydroperoxylinoleic acid/linoleic acid fatty acid dimers containing conjugated double bonds were formed additionally. The pea enzyme showed self-inactivation at 37 degrees C, but in contrast to the lipoxygenase from rabbit reticulocytes the self-inactivation appeared only syncatalytically during the aerobic reaction. The antioxidant 2,6-di-t-butyl-4-hydroxytoluene (BHT, 1 mM) did not protect from self-inactivation. In contrast to the lipoxygenase from soybeans, wheat and rabbit reticulocytes the pea lipoxygenase caused a co-oxidation of Cu-chlorophyllin in the presence of linoleate at 5 degrees C. The co-oxidation was completely inhibited by 1 mM BHT which did not inhibit the dioxygenation of linoleate at this temperature. Unlike the reticulocyte enzyme the pea lipoxygenase failed to attack mitochondrial membranes or to produce inhibition of the respiratory chain. The results lead to the conclusion that a simple classification of lipoxygenases in type I and type II enzymes is not justified. A reaction scheme is proposed to explain both the co-oxidative activity and the aerobic formation of oxodienoic acids by pea lipoxygenase, presuming the dissociation of a linoleic acid radical from the ferrous lipoxygenase as a side reaction of the catalytic cycle.

Animals↗

Requirements for non-food applications of pea proteins. A review.

So far, limited research is performed on technical applications of pea proteins and no applications have yet been reported. At ATO, three technical applications were investigated: surfactants, films, and microspheres as encapsulation matrices. Pea protein hydrolysates are surfactants with good emulsifying and foaming properties. By variation of enzyme type and degree of hydrolysis, the surfactant properties can be tailored toward specific applications. Pea protein films could be prepared by casting from dispersions at pH 7 and 10, and by compression moulding at 140 degrees C. Opposite to many other proteins, pea protein films combine strength (5-7.5 MPa) with high elongation at break (150%). A protein isolate derived from peas was applied as matrix material for the microencapsulation of beta-carotene, intended for cosmetic applications. Supercritical CO2 technology appeared to be a promising encapsulation technique for beta-carotene in porous pea protein microspheres. Advantages of this method are that no organic solvents are used, and that encapsulation is achieved under mild conditions, thereby preventing the sensitive beta-carotene from degradation.

Biofilms↗

Expression dynamics of the pea rbcS multigene family and organ distribution of the transcripts.

We have determined the nucleotide sequence of two members (rbcS-3A and -3C) of the pea nuclear gene family encoding the small subunit (rbcS) of ribulose-1,5-bisphosphate carboxylase. Both rbcS-3A and -3C are interrupted by two introns located at the same positions as those of the other three pea rbcS genes. Compared with the other pea rbcS genes the rbcS-3C gene has the most divergent 5'- and 3'-flanking sequences while the rbcS-3A gene has a larger and highly divergent intron 1. All five pea rbcS genes are conserved in their coding regions but show considerable sequence differences in their 3'-untranslated portion. The 3' sequence divergence of the rbcS genes has allowed us to use S1 nuclease mapping procedures to compare their expression levels in different organs and during light induction. All the rbcS genes are differentially expressed in various organs of the pea plants; moreover, specific rbcS transcripts are under-represented in seeds and petals. In leaves there is a 10-fold difference between the highest and lowest specific rbcS transcript levels. By quantitating the distribution of rbcS transcripts during light, phytochrome and blue light induction of immature (etiolated), and mature (green), pea leaves, we show that the genes are differentially activated during leaf development.

Journal Article↗

Molecular cloning of isoflavone reductase from pea (Pisum sativum L.): evidence for a 3R-isoflavanone intermediate in (+)-pisatin biosynthesis.

Isoflavone reductase (IFR) reduces achiral isoflavones to chiral isoflavanones during the biosynthesis of chiral pterocarpan phytoalexins. A cDNA clone for IFR from pea (Pisum sativum) was isolated using the polymerase chain reaction and expressed in Escherichia coli. Analysis of circular dichroism (CD) spectra of the reduction product sophorol obtained using the recombinant enzyme indicated that the isoflavanone possessed the 3R stereochemistry, in contrast to previous reports indicating a 3S-isoflavanone as the product of the pea IFR. Analysis of CD spectra of sophorol produced using enzyme extracts of CuCl2-treated pea seedlings confirmed the 3R stereochemistry. Thus, the stereochemistry of the isoflavanone intermediate in (+)-pisatin biosynthesis in pea is the same as that in (-)-medicarpin biosynthesis in alfalfa, although the final pterocarpans have the opposite stereochemistry. At the amino acid level the pea IFR cDNA was 91.8 and 85.2% identical to the IFRs from alfalfa and chickpea, respectively. IFR appears to be encoded by a single gene in pea. Its transcripts are highly induced in CuCl2-treated seedlings, consistent with the appearance of IFR enzyme activity and pisatin accumulation.

Amino Acid Sequence↗

Pea chloroplast DNA primase: characterization and role in initiation of replication.

A DNA primase activity was isolated from pea chloroplasts and examined for its role in replication. The DNA primase activity was separated from the majority of the chloroplast RNA polymerase activity by linear salt gradient elution from a DEAE-cellulose column, and the two enzyme activities were separately purified through heparin-Sepharose columns. The primase activity was not inhibited by tagetitoxin, a specific inhibitor of chloroplast RNA polymerase, or by polyclonal antibodies prepared against purified pea chloroplast RNA polymerase, while the RNA polymerase activity was inhibited completely by either tagetitoxin or the polyclonal antibodies. The DNA primase activity was capable of priming DNA replication on single-stranded templates including poly(dT), poly(dC), M13mp19, and M13mp19 + 2.1, which contains the AT-rich pea chloroplast origin of replication. The RNA polymerase fraction was incapable of supporting incorporation of 3H-TTP in in vitro replication reactions using any of these single-stranded DNA templates. Glycerol gradient analysis indicated that the pea chloroplast DNA primase (115-120 kDa) separated from the pea chloroplast DNA polymerase (90 kDa), but is much smaller than chloroplast RNA polymerase. Because of these differences in size, template specificity, sensitivity to inhibitors, and elution characteristics, it is clear that the pea chloroplast DNA primase is an distinct enzyme form RNA polymerase. In vitro replication activity using the DNA primase fraction required all four rNTPs for optimum activity. The chloroplast DNA primase was capable of priming DNA replication activity on any single-stranded M13 template, but shows a strong preference for M13mp19 + 2.1. Primers synthesized using M13mp19 + 2.1 are resistant to DNase I, and range in size from 4 to about 60 nucleotides.

Antibodies↗

Hormonal regulation of S-adenosylmethionine synthase transcripts in pea ovaries.

Two cDNA clones coding for S-adenosyl-L-methionine synthase (SAMs, EC 2.5.1.6) have been isolated from a cDNA library of gibberellic acid-treated unpollinated pea ovaries. Both cDNAs were sequenced showing a high degree of identity but coding for different SAMs polypeptides. The presence of two SAMs genes in pea was further confirmed by Southern analysis. Expression of the SAMs genes in the pea plant was found at different levels in vegetative and reproductive tissues. We characterized the expression levels of SAMs genes during the development or senescence of pea ovaries. Northern analysis showed that transcription of SAMs genes in parthenocarpic fruits was upregulated by auxins in the same manner as in fruits from pollinated ovaries. In both pollinated and 2,4-dichlorophenoxyacetic acid-treated ovaries, and benzyladenine, although able to induce parthenocarpic development, did not affect SAMs mRNA levels. These data are consistent with an active participation of auxins in the upregulation of SAMs during fruit setting in pea and suggest that, at the molecular level, parthenocarpic development of pea ovaries is different for gibberellin- and cytokinin-treated ovaries than for auxin-induced parthenocarpic biosynthesis since treatment of the ovaries with aminoethoxyvinylglycine resulted in a delay of senescence and prevention of SAMs mRNA accumulation. A possible mechanism for hormonal regulation of SAMs during ovary development is discussed.

Aging↗

The beta-tubulin gene family of pea: primary structures, genomic organization and intron-dependent evolution of genes.

One gene and two cDNAs encoding three different beta-tubulins (TUB1, TUB2, TUB3) of pea have been cloned and sequenced. The derived amino acid sequences show between 92% and 96% identity relative to one another and to most other beta-tubulins of higher plants and green algae. Two notable extremes are the high similarity of 98% between pea TUB3 and maize beta-tubulin 2 and the relatively low similarity (90%) of the hypocotyl-specific beta-tubulin 1 of soybean to the pea sequences. These similarities do not reflect the molecular phylogeny but rather differences in evolutionary rate of beta-tubulins which are differentially regulated during plant development. Genomic Southern blots reveal a beta-tubulin gene family in pea with at least four separate members including two TUB1 genes, one TUB2 gene and one TUB3 gene. This contradicts an earlier report by Raha et al. (Plant Mol Biol 9: 565-571, 1987) suggesting a tandem repeat organization of tubulin genes in pea. The pea TUB1 gene has two introns in identical positions compared to the beta-tubulin genes from Arabidopsis and soybean. In an attempt to reconstruct the universal ancestor of all present-day tubulin genes the intron positions in 38 different alpha- and beta-tubulin genes from plants, animals, fungi and protozoa were compared. This comparison shows that the primordial gene probably had many introns (more than 20) separating 'protoexons' of 15 to 20 codons in agreement with the 'exon theory of genes'. It also supports the view that, during the course of evolution, introns have shifted and were deleted preferentially in the 3' part of the genes. Similar observations have been made previously for other genes. They can be interpreted in terms of a homologous recombination of genes with their modified (incorrectly spliced) and reverse-transcribed pre-mRNAs.

Amino Acid Sequence↗

Protein quality traits of vegetable and field peas: varietal differences.

Four high yielding varieties of field (Rachna and RFP4) and vegetable peas (Bonnivielle and Arkal) were studied for their protein quality. Crude protein and true protein content of all four pea varieties varied from 19.5 to 20.6 percent and 18.7 to 19.8 percent, respectively. Non protein nitrogen formed only 3.94 to 4.84 percent of total nitrogen. Globulins were the major fractions followed by albumins and glutelins. All the four varieties of peas had similar methionine and tryptophan content. Lysine content of four pea varieties ranged from 7.56 to 9.65 g per 16 g of N. Cooking brought about an increase in in vitro protein digestibility of peas by 10 percent. The sodium dodecyl polyacrylamide gel electrophoresis of total protein revealed the presence of 22-25 bands with some difference in banding pattern of all four varieties. Some differences were observed in banding patterns of globulin and albumin of all four varieties, suggesting that composition of protein of pea varieties differed.

Albumins↗

Gastric mucosal protection with beta-phenylethylamine (PEA) and other sympathomimetic amines against absolute ethanol in the rat.

The purpose of this study was to investigate the potential of beta-phenylethylamine (PEA), an amphetamine-like compound present in the blood during high stress situations, to protect rat gastric mucosa against absolute ethanol. F-344 rats were pretreated with PEA in saline at several dose levels and at various times prior to oral administration of 1 ml absolute ethanol. PEA at dose levels of 50 and 100 mg/kg significantly reduced the severity of alcohol-induced lesions following oral, but not parenteral, treatment. The duration of protection with PEA was approximately 90 min, with maximum protection observed when PEA was administered 15-30 min before alcohol. Pretreatment with indomethacin did not prevent or reduce the protection induced by PEA. Other sympathomimetic amines such as isoproterenol and ephedrin were similarly cytoprotective against absolute ethanol while amphetamine, phenylephrine, and epinephrine proved ineffective. These results add further support to the role of the sympathetic nervous system in regulating gastric mucosal protection in the rat.

Amines↗

The isolation and purification of diamine oxidase of pea seedlings and pig liver.

Enzymes have been extensively used in many industries for the last 20 years. They are becoming more common because of new areas of application. The limitations of applications of enzymes are activity, specificity, stability, and price. Higher enzyme activities and less susceptibility of process conditions are desirable. Therefore, in some cases, purified enzyme extracts are needed. The purpose of this study is the isolation and purification of diamine oxidase (DAO) of pea seedlings and pig liver. The relationship between pea seedlings growth rate and enzyme activity is established. DAO of pea seedlings and pig liver is prepared by way of tissue disruption with homogenization, centrifugation, fractionation with ammonium sulfate, precipitation of inert components, column electrophoresis, and DEAE-cellulose column chromatography. The specific activity of disrupted pea seedlings cells was measured as 0.017 (U/mg protein), and the pig liver DAO activity was measured as 0.00037 (U/mg protein). The specific enzyme activity from pea seedlings was increased to 6.750 (U/mg protein). On the other hand, the specific enzyme activity from pig liver was increased to 0.30 (U/mg protein). The final enzyme extract from pea is 400-fold purer than raw material, and the final enzyme extract from pig liver is 820-fold purer than raw material.

Amine Oxidase (Copper-Containing)↗

Genome wide association study unveils the genetic basis of Orobanche crenata resistance in pea.

GWAS using DArTseq markers identified novel resistance sources against parasitic broomrape in pea, elucidating candidate genes for marker-selected breeding as leverage for cultivar development and efficient disease control to enhance food security. Crenate broomrape (Orobanche crenata) is an important obligate root parasitic weed that causes severe yield losses in pea (Pisum sativum) production. O. crenata is difficult to eradicate in pea fields due to its high resilience and prolific seed boom capable of hibernating in soils for decades. Existing control strategies are not cost effective in low input legumes like pea. The most efficient ecofriendly mode of control is using resistant cultivars. Quantitative trait loci (QTL) studies based on bi-parental mapping has guided O. crenata resistance discovery, albeit their deployment in pea breeding is hindered by low marker resolution and large genetic distance. This study presents the first genome-wide association study (GWAS) on O. crenata resistance in pea, utilizing 324 diverse accessions and 26,045 diversity array technology sequence (DArTseq) markers. Phenotyping was performed over four seasons under field conditions using alpha lattice design. Results showed a strong phenotypic variation with an environmental influence on O. crenata infection. Novel resistance sources were identified mainly within the wild Pisum fulvum and P. sativum subsp. elatius. GWAS with two models yielded a total of 73 marker-trait associations with Chromosome 5 as major hotspot. Interestingly, some linked markers were detected in close proximity to four previous O. crenata resistance QTL. DArTseq markers identified 24 putative candidate genes participating in different cellular processes, including vesicle trafficking and transports, deoxyribonucleic acid transcription regulation, and defense including some leucine rich repeat receptor-like kinases. These results provide a valuable genetic resource for O. crenata resistance and a step toward its effective sustainable management-to enhance genetic diversity and cultivar improvement for food security.

Pisum sativum↗

Beta-ketoacyl-acyl carrier protein synthase III from pea (Pisum sativum L.): properties, inhibition by a novel thiolactomycin analogue and isolation of a cDNA clone encoding the enzyme.

A beta-ketoacyl-acyl carrier protein (ACP) synthase III (KAS III; short-chain condensing enzyme) has been partly purified from pea leaves. The enzyme, which had acetyl-CoA:ACP acyltransferase (ACAT) activity, was resolved from a second, specific, ACAT protein. The KAS III enzyme had a derived molecular mass of 42 kDa (from its cDNA sequence) and operated as a dimer. Its enzymological characteristics were similar to those of two other plant KAS III enzymes except for its inhibition by thiolactomycin. A derivative of thiolactomycin containing a longer (C8 saturated) hydrophobic side-chain (compound 332) was a more effective inhibitor of pea KAS III and showed competitive inhibition towards malonyl-ACP whereas thiolactomycin showed uncompetitive characteristics at high concentrations. This difference may be due to the better fit of compound 332 into a hydrophobic pocket at the active site. A full-length cDNA for the pea KAS III was isolated. This was expressed in Escherichia coli as a fusion protein with glutathione S-transferase in order to facilitate subsequent purification. Demonstrated activity in preparations from E. coli confirmed that the cDNA encoded a KAS III enzyme. Furthermore, the expressed KAS III had ACAT activity, showing that the latter was inherent. The derived amino acid sequence of the pea cDNA showed 81-87% similarity to that for other plant dicotyledon KAS IIIs, somewhat less for Allium porrum (leek, 71%) and for Porphyra spp. (62%), Synechocystis spp. (65%) and various bacteria (42-65%). The pea KAS III exhibited four areas of homology, three of which were around the active-site Cys(123), His(323) and Asn(353). In addition, a stretch of 23 amino acids (residues 207-229 in the pea KAS III) was almost completely conserved in the plant KAS IIIs. Modelling this stretch showed they belonged to a peptide fragment that fitted over the active site and contained segments suggested to be involved in substrate binding and in conformational changes during catalysis, as well as an arginine suggested to participate in the acid-base catalytic mechanism.

3-Oxoacyl-(Acyl-Carrier-Protein) Synthase↗

Auxin-cytokinin and auxin-gibberellin interactions during morphogenesis of the compound leaves of pea (Pisum sativum).

A number of mutations that alter the form of the compound leaf in pea (Pisum sativum) has proven useful in elucidating the role that auxin might play in pea leaf development. The goals of this study were to determine if auxin application can rescue any of the pea leaf mutants and if gibberellic acid (GA) plays a role in leaf morphogenesis in pea. A tissue culture system was used to determine the effects of various auxins, GA or a GA biosynethesis inhibitor (paclobutrazol) on leaf development. The GA mutant, nana1 (na1) was analyzed. The uni-tac mutant was rescued by auxin and GA and rescue involved both a conversion of the terminal leaflet into a tendril and an addition of a pair of lateral tendrils. This rescue required the presence of cytokinin. The auxins tested varied in their effectiveness, although methyl-IAA worked best. The terminal tendrils of wildtype plantlets grown on paclobutrazol were converted into leaflets, stubs or were aborted. The number of lateral pinna pairs produced was reduced and leaf initiation was impaired. These abnormalities resembled those caused by auxin transport inhibitors and phenocopy the uni mutants. The na1 mutant shared some morphological features with the uni mutants; including, flowering late and producing leaves with fewer lateral pinna pairs. These results show that both auxin and GA play similar and significant roles in pea leaf development. Pea leaf morphogenesis might involve auxin regulation of GA biosynthesis and GA regulation of Uni expression.

Benzyl Compounds↗

Pea chloroplast FtsZ can form multimers and correct the thermosensitive defect of an Escherichia coli ftsZ mutant.

This paper reports the isolation and characterization of a cDNA encoding the FtsZ protein of pea. The protein is synthesised as a precursor molecule of 423 amino acids with a molecular mass of 44 kDa. When translated in vitro, the protein is translocated efficiently into isolated, intact pea chloroplasts, demonstrating that the protein is localised in the chloroplast. Pea FtsZ synthesised in vitro formed multimers in a calcium-dependent manner. The pea cDNA complemented the thermosensitive defect of an E. coli ftsZ mutant in vivo and converted the filamentous phenotype of the E. coli mutant into the normal wild-type morphology at 42 degrees C. However, pea FtsZ mutants that were defective in multimerisation in vitro failed to correct the phenotype of the E. coli ftsZ mutant in vivo. The pea ftsZ transcripts were abundantly present in the young leaves, but barely detectable in roots and stems and undetectable in older leaves. Light stimulated transcription of the gene significantly in young and dark-grown leaves. This study strongly suggests that the division mechanisms used by chloroplasts and bacteria show considerable similarity.

Bacterial Proteins↗

A comparative immunocytochemical study using an antiserum against a synthetic analogue of the corpora cardiaca peptide Pea-CAH-I (MI, neurohormone D) of Periplaneta americana.

An antiserum against the octapeptide Pea-CAH-I, a member of the adipokinetic hormone/red pigment-concentrating hormone family, has been produced for immunocytochemical staining in insects and various other invertebrate species. The anti-Pea-CAH-I serum stains the glandular corpora cardiaca cells of those insect species that synthesize identical or structurally similar peptides. In the corpora cardiaca of species producing peptides with a different C-terminus, these cells remain unstained. Pea-CAH-I-like immunoreactivity has also been found in neurons of the central nervous system of all invertebrate orders studied. The antiserum recognizes the C-terminal sequence Pro-Asn-Trp-NH2 of the Pea-CAH-I molecule as established by enzyme immunoassay. The widespread Pea-CAH-I-like immunoreactivity in all nervous systems of the studied animals probably does not reflect the presence of Pea-CAH-I but the occurrence of peptides carrying similar epitopes.

Amino Acid Sequence↗

Antagonism by CPP (+/-)-3-(2-carboxypiperazin-4-yl)-propyl-1-phosphonic acid, of beta-phenylethylamine (PEA)-induced hypermotility in mice of different strains.

In male C57BL/6, BALB/c, and SHR (bred from Swiss) mice, pretreatment with (+/-)-3-(2-carboxypiperazin-4-yl)-propyl-1-phosphonic acid (CPP), a competitive antagonist of N-methyl-D-aspartate (NMDA) receptor, attenuated the hyperlocomotion induced by beta-phenylethylamine (PEA). This effect of CPP was blocked by intracerebroventricularly (ICV) administered NMDA (0.2 nM). CPP did not alter the hyperlocomotion induced by d-amphetamine. PEA rarely inhibited spontaneous motor activity in those strains. Two other competitive antagonists of NMDA, 2-amino-5-phosphonopentanoic acid (AP-5) and 2-amino-7-phosphonoheptanoic acid (AP-7), ICV at doses of 0.01-0.1 microgram, were ineffective. The noncompetitive antagonists of NMDA, dizocilpine (MK-801) and phencyclidine, at subthreshold doses of 0.1-0.5 mg/kg, potentiated the stimulant effect of PEA. In earlier studies we also observed antagonism between CPP and PEA in NIH-Swiss mice, a strain in which PEA inhibits locomotion. Relationships between the stimulant and the anxiogenic effects of PEA are discussed.

Animals↗

Quantifying ERK2-protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains.

While mitogen-activated protein kinase signaling pathways constitute highly regulated networks of protein-protein interactions, little quantitative information for these interactions is available. Here we highlight recent fluorescence anisotropy binding studies that focus on the interactions of ERK1 and ERK2 with PEA-15 (antiapoptotic phosphoprotein enriched in astrocytes-15 kDa), a small protein that sequesters ERK2 in the cytoplasm. The regulation of ERK2 by PEA-15 is appraised in the light of a simple equilibrium-binding model for reversible ERK2 nucleoplasmic-cytoplasmic shuttling, which elaborates on the theory of Burack and Shaw (J. Biol. Chem. 280, 3832-3837; 2005). Also highlighted is the recent observation that the peptide N-QKGKPRDLELPLSPSL-C, derived from the docking site for ERK/JNK and LEL (DEJL) in Elk-1, displaces PEA-15 from ERK2. It is proposed that the C-terminus of PEA-15 ((121)LXLXXXXKK(129)) is a reverse DEJL domain [which has a general consensus of R/K-phi(A)-X(3/4)-phi(B), where phi(A) and phi(B) are hydrophobic residues (Leu, Ile, or Val)], which mediates one arm of a bidentate PEA-15 interaction with ERK2. The notion that PEA-15 is a potent inhibitor of many ERK2-mediated phosphorylations, by virtue of its ability to block ERK2-DEJL domain interactions, is proposed.

Active Transport, Cell Nucleus↗