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PubMed1982

Control of storage-protein synthesis during seed development in pea (Pisum sativum L.).

The tissue-specific syntheses of seed storage proteins in the cotyledons of developing pea (Pisum sativum L.) seeds have been demonstrated by estimates of their qualitative and quantitative accumulation by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and rocket immunoelectrophoresis respectively. Vicilin-fraction proteins initially accumulated faster than legumin, but whereas legumin was accumulated throughout development, different components of the vicilin fraction had their predominant periods of synthesis at different stages of development. The translation products in vitro of polysomes isolated from cotyledons at different stages of development reflected the synthesis in vivo of storage-protein polypeptides at corresponding times. The levels of storage-protein mRNA species during development were estimated by 'Northern' hybridization using cloned complementary-DNA probes. This technique showed that the levels of legumin and vicilin (47000-Mr precursors) mRNA species increased and decreased in agreement with estimated rates of synthesis of the respective polypeptides. The relative amounts of these messages, estimated by kinetic hybridization were also consistent. Legumin mRNA was present in leaf poly(A)+ RNA at less than one-thousandth of the level in cotyledon poly(A)+ (polyadenylated) RNA, demonstrating tissue-specific expression. Evidence is presented that storage-protein mRNA species are relatively long-lived, and it is suggested that storage-protein synthesis is regulated primarily at the transcriptional level.

DNA↗
PubMed2000

Expression and parent-of-origin effects for FIS2, MEA, and FIE in the endosperm and embryo of developing Arabidopsis seeds.

The promoters of MEA (FIS1), FIS2, and FIE (FIS3), genes that repress seed development in the absence of pollination, were fused to beta-glucuronidase (GUS) to study their activity pattern. The FIS2GUS product is found in the embryo sac, in each of the polar cell nuclei, and in the central cell nucleus. After pollination, the maternally derived FIS2GUS protein occurs in the nuclei of the cenocytic endosperm. Before cellularization of the endosperm, activity is terminated in the micropylar and central nuclei of the endosperm and subsequently in the nuclei of the chalazal cyst. MEAGUS has a pattern of activity similar to that of FIS2GUS, but FIEGUS protein is found in many tissues, including the prepollination embryo sac, and in embryo and endosperm postpollination. The similarity in mutant phenotypes; the activity of FIE, MEA, and FIS2 in the same cells in the embryo sac; and the fact that MEA and FIE proteins interact in a yeast two-hybrid system suggest that these proteins operate in the same system of control of seed development. Maternal and not paternal FIS2GUS, MEAGUS, and FIEGUS show activity in early endosperm, so these genes may be imprinted. When fis2, mea, and fie mutants are pollinated, seed development is arrested at the heart embryo stage. The seed arrest of mea and fis2 is avoided when they are fertilized by a low methylation parent. The wild-type alleles of MEA or FIS2 are not required. The parent-of-origin-determined differential activity of MEA, FIS2, and FIE is not dependent on DNA methylation, but methylation does control some gene(s) that have key roles in seed development.

Arabidopsis↗
PubMed1967

Ribonuclease activity in the developing seeds of normal and opaque-2 maize.

During development, the ribonuclease activity of maize endo sperm homozygous for the opaque-2 gene increased earlier and, after a longer period of exponential increase, was much higher finally than in normal endosperm. The maximum difference was about sixfold and occurred 22 to 25 days after pollination. Heterozygotes on day 23 did not show a comparable in crease in endosperm activity. No differ ence in the activity ratio (pH 6.0: pH 5.2) was found between normal and opaque-2 endosperm, indicating that the increase in activity in opaque-2 was due solely to an increase in ribo nuclease A. The ribonuclease activity of opaque-2 embryos increased more rapidly than that of normal embryos, but the final activity was the same in each case.

In Vitro Techniques↗
PubMed2001

Arabidopsis glucosidase I mutants reveal a critical role of N-glycan trimming in seed development.

Glycoproteins with asparagine-linked (N-linked) glycans occur in all eukaryotic cells. The function of their glycan moieties is one of the central problems in contemporary cell biology. N-glycosylation may modify physicochemical and biological protein properties such as conformation, degradation, intracellular sorting or secretion. We have isolated and characterized two allelic Arabidopsis mutants, gcs1-1 and gcs1-2, which produce abnormal shrunken seeds, blocked at the heart stage of development. The mutant seeds accumulate a low level of storage proteins, have no typical protein bodies, display abnormal cell enlargement and show occasional cell wall disruptions. The mutated gene has been cloned by T-DNA tagging. It codes for a protein homologous to animal and yeast alpha-glucosidase I, an enzyme that controls the first committed step for N-glycan trimming. Biochemical analyses have confirmed that trimming of the alpha1,2- linked glucosyl residue constitutive of the N-glycan precursor is blocked in this mutant. These results demonstrate the importance of N-glycan trimming for the accumulation of seed storage proteins, the formation of protein bodies, cell differentiation and embryo development.

Alleles↗
PubMed2005

Sugar metabolism in developing lupin seeds is affected by a short-term water deficit.

A short-term water deficit (WD) imposed during the pre-storage phase of lupin seed development [15-22 d after anthesis (DAA)] accelerated seed maturation and led to smaller and lighter seeds. During seed development, neutral invertase (EC 3.2.1.26) and sucrose synthase (EC 2.4.1.13) have a central role in carbohydrate metabolism. Neutral invertase is predominant during early seed development (up to 40 DAA) and sucrose synthase during the growing and storage phase (40-70 DAA). The contribution of acid invertase is marginal. WD decreased sucrose synthase activity by 2-fold and neutral invertase activity by 5-6-fold. These changes were linked to a large decrease in sucrose ( approximately 60%) and an increase of the hexose:sucrose ratio. Rewatering restored sucrose synthase activity to control levels while neutral invertase activity remained depressed (30-60%). A transient accumulation of starch observed in control seeds was abolished by WD. Despite the several metabolic changes the final seed composition was largely unaltered by WD except for approximately 60% increase in stachyose and raffinose (raffinose family oligosaccharides). This increase in raffinose family oligosaccharides appears as the WD imprinting on mature seeds.

Carbohydrate Metabolism↗
PubMed1995

Molecular characterization of cDNAs corresponding to genes expressed during almond (Prunus amygdalus Batsch) seed development.

A number of different cDNA clones corresponding to the most abundant mRNAs present in immature seeds have been isolated from an almond (Prunus amygdalus cv. Texas) immature seed cDNA library. Those corresponding to proteins involved in storage processes have been further characterized. Two of these cDNAs (PA3BF1 and PA3BE12) code for the almond globulins (prunins), the main family of storage proteins synthesized in seeds during embryogenesis, and another cDNA (PA3BA1) codes for the 15.7 kDa almond oleosin, a protein located on the surface of oil bodies in plant seeds. These cDNAs have been sequenced and their expression during almond fruit development has been studied. Their expression is seed-specific and localized in cotyledons around 100 days after flowering. Both prunin and oleosin genes are present in one or two copies in the almond genome.

Amino Acid Sequence↗
PubMed1996

Sucrose metabolism during cotyledon development of Vicia faba L. is controlled by the concerted action of both sucrose-phosphate synthase and sucrose synthase: expression patterns, metabolic regulation and implications for seed development.

The roles of sucrose-phosphate synthase (Sps) and sucrose synthase (Sus) in developing embryos of Vicia faba have been characterized. In the cotyledons the expression of both Sps and Sus is initiated in cells differentiating into storage tissue. This stage is characterized by a switch in the carbohydrate state from a high to a low hexoses to sucrose ratio. The carbohydrate state was found earlier to be controlled by seed coat-associated invertase. During cotyledon development the Sps-enzyme undergoes a cycle of deactivation and reactivation: the activated state is associated with the prestorage phase, desiccation and germination and the deactivated state with the storage phase. Sus activity is associated with the storage phase. Sps and Sus are differentially influenced by free sugars. Feeding hexoses to storage phase cotyledons increases levels of Sps-mRNA but not Sus-mRNA, Sps activity and Sps activation state and impairs storage functions evidenced by an increased sucrose to starch ratio and a downregulation of storage protein legumin B-mRNA. Sus enzyme activity is inhibited by free hexoses in vitro. It is proposed that the changing carbohydrate state during cotyledon development controls the ratio of Sps to Sus. Sps may have some significance for the initiation of the storage process possibly decreasing hexoses and/or increasing sucrose. The relevance of the changing carbohydrate state with respect to development and storage processes is discussed.

Base Sequence↗
PubMed1998

Purification and characterization of a low-molecular-weight phospholipase A2 from developing seeds of elm.

Phospholipase A2 (PLA2) was purified about 180,000 times compared with the starting soluble-protein extract from developing elm (Ulmus glabra) seeds. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis the purified fraction showed a single protein band with a mobility that corresponded to 15 kD, from which activity could be recovered. When analyzed by matrix-assisted laser-desorption ionization-time-of-flight mass spectrometry, the enzyme had a deduced mass of 13,900 D. A 53-amino acid-long N-terminal sequence was determined and aligned with other sequences, giving 62% identity to the deduced amino acid sequence of some rice (Oryza sativa) expressed sequence tag clones. The purified enzyme had an alkaline pH optimum and required Ca2+ for activity. It was unusually stable with regard to heat, acidity, and organic solvents but was sensitive to disulfide bond-reducing agents. The enzyme is a true PLA2, neither hydrolyzing the sn-1 position of phosphatidylcholine nor having any activity toward lysophosphatidylcholine or diacylglycerol. The biochemical data and amino acid sequence alignments indicate that the enzyme is related to the well-characterized family of animal secretory PLA2s and, to our knowledge, is the first plant enzyme of this type to be described.

Amino Acid Sequence↗
PubMed2002

High expression of putative aquaporin genes in cells with transporting and nutritive functions during seed development in Norway spruce (Picea abies).

Aquaporins mediate the bidirectional passage of water over membranes and are present in tonoplasts (TIPs) and in plasma membranes (PIPs) of plant cells. Knowing their expression in different tissues is valuable when assessing their contribution to plant water relations. A TIP-gene has been cloned from developing female gametophytes of Picea abies, a conifer displaying an embryology different from the angiosperms. Probes were made from conserved regions of the TIP gene and used for in situ hybridization to examine the gene expression pattern in developing female reproductive structures. Early during development high transcript expression was found in the spongy tissue encasing the developing female gametophyte, in cells of the future seed coat of young ovules and in vascular tissue of the ovuliferous scale. At later stages a strong signal was seen in archegonia jacket cells surrounding egg cells and, still later, at the time of storage protein accumulation, in storage parenchyma cells of the gametophyte as well. These aquaporin-homologues probably participate in regulating water balance in the cells although they could also be permeable to other molecules than water.

Amino Acid Sequence↗
PubMed1982

Biosynthesis of storage proteins in developing rice seeds.

Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis of the starchy endosperm protein of rice (Oryza sativa L. Japonica cv Koshihikari) during seed development confirmed that storage protein begins to accumulate about 5 days after flowering. Two polypeptide groups, 22 to 23 and 37 to 39 kilodaltons, the components of glutelin, the major storage protein in rice seed, appeared 5 days after flowering. A 26-kilodalton polypeptide, the globulin component, also appeared 5 days after flowering. Smaller polypeptides (10- to 16-kilodaltons) including prolamin components, appeared about 10 days after flowering. In contrast, the levels of the 76- and 57-kilodalton polypeptides were fairly constant throughout seed development. Transmission electron microscopy and fractionation by sucrose density gradient centrifugation of the starchy endosperms at various stages of development showed that protein body type II, the accumulation site of glutelin and globulin, was formed faster than protein body type I, the accumulation site of prolamin.The 57-kilodalton polypeptide but not the glutelin subunits was labeled in a 2-hour treatment with [(14)C]leucine given between 4 and 12 days after flowering to developing ears. In vivo pulse-chase labeling studies showed the 57-kilodalton polypeptide to be a precursor of the 22 to 23 and 37 to 39 kilodalton subunits. The 57-kilodalton polypeptide was salt-soluble, but the mature glutelin subunits were almost salt insoluble.In vitro protein synthesis also showed that the mRNAs directly coding the 22 to 23 and 37 to 39 kilodalton components were absent in developing seeds and that the 57-kilodalton polypeptide was the major product. Thus, it was concluded that the two subunits of rice glutelin are formed through post-translational cleavage of the 57-kilodalton polypeptide.

Journal Article↗
PubMed1995

cDNA cloning for a putative cysteine proteinase from developing seeds of soybean.

cDNA clones for a putative cysteine proteinase were isolated from developing cotyledons of soybean (Glycine max.) using PCR-based techniques. The full-length clone of 1441 bp encodes a proteinase pre-propolypeptide of 380 amino acids. It belongs to the commonly known papain family and shows the highest sequence homology (up to 53% identity) to the protein 15A, a turgor-responsive cysteine proteinase of pea, as well as to several other stress inducible proteinases. Biosynthesis of the corresponding transcripts was shown to be developmentally controlled during embryogenesis. Southern analyses revealed occurrence of one to two genes in the soybean genome.

Amino Acid Sequence↗
PubMed1990

Seed Development in Phaseolus vulgaris L. cv Seminole: II. Precocious Germination in Late Maturation.

Seeds of Phaseolus vulgaris L. cv Seminole in late maturation phase germinated precociously in vitro. Germination occurred in the absence of free water after 5 days but within 24 to 48 hours in contact with water. Excised axes germinated within 12 hours and embryos by 48 hours only if supplied with water. Ethylene accelerated the germination of seeds and embryos irrespective of water availability. There was no effect of ethylene on the rate of axis germination. Ethylene was equally effective within the range 0.5 to 1000 parts per million and 1 hour exposure was fully effective. Induction of precocious germination in vivo was observed by manipulating water content inside pods or by ethylene injection, whether pods were attached to the parent plant or not. These results demonstrate the importance of endogenous regulation of water supply in suppressing precocious germination. Ethylene is identified as a powerful antagonist to the natural control.

Journal Article↗
PubMed2003

Lipid storage metabolism is limited by the prevailing low oxygen concentrations within developing seeds of oilseed rape.

The aim of this study was to investigate whether endogenous restrictions in oxygen supply are limiting for storage metabolism in developing oilseed rape (Brassica napus) seeds. Siliques were studied 30 d after flowering, when rapid lipid accumulation is occurring in the seeds. (a). By using microsensors, oxygen concentrations were measured within seeds and in the silique space between seeds. At ambient external oxygen (21% [v/v]) in the light, oxygen fell to 17% (v/v) between and 0.8% (v/v) within seeds. A step-wise reduction of the external oxygen concentration led within 2 h to a further decrease of internal oxygen concentrations, and a step-wise increase of the external oxygen concentration up to 60% (v/v) resulted in an increase in internal oxygen that rose to 30% (v/v) between and 8% (v/v) within seeds. (b). The increase in oxygen levels in the seeds was accompanied by a progressive increase in the levels of ATP, UTP, and the ATP to ADP and UTP to UDP ratios over the entire range from 0% to 60% (v/v) external oxygen. (c). To investigate metabolic fluxes in planta, 14C-sucrose was injected into seeds, which remained otherwise intact within their siliques. The increase in oxygen in the seeds was accompanied by a progressive increase in the rate of lipid (including triacylglycerol), protein and cell wall synthesis, and an increase in glycolytic flux over a range from sub- to superambient oxygen concentrations. In contrast to lipid synthesis, starch synthesis was not significantly increased at superambient oxygen levels. The levels of fermentation products such as lactate and glycerol-3P increased only at very low (0%-4% [v/v]) external oxygen concentrations. (d). When 14C-acetate or 14C-acetyl-coenzyme A (CoA) was injected into seeds, label incorporation into triacylglycerol progressively increased over the whole range of external oxygen concentrations from 0% to 60% (v/v). (e). Stimulation of lipid synthesis was accompanied by an increase in sugar levels and a decrease in the levels of hexose-phosphates and acetyl-CoA, indicating sucrose unloading and the use of acetyl-CoA as possible regulatory sites. (f). Increased lipid synthesis was also accompanied by an increase in the maximal activities of invertase and diacylglycerol acyltransferase. (g). The developmental shift from starch to lipid storage between 15 and 45 d after flowering was accompanied by an increase in the seed energy state. (h). The results show that at ambient oxygen levels, the oxygen supply is strongly limiting for energy metabolism and biosynthetic fluxes in growing rape seeds, affecting lipid synthesis more strongly than starch synthesis. The underlying mechanisms and implications for strategies to increase yield and storage product composition in oilseed crops are discussed.

Acetates↗
PubMed1979

Nature and Patterns of Proteins during Cotton Seed Development.

Patterns of accumulation and ontogenetic relationships among proteins of cotton (Gossypium hirsutum L.) seeds were examined between 10 days postanthesis and maturity (56 days). Total and extractable nitrogen contents were determined; alkali- and water-soluble proteins were assayed quantitatively and electrophoretically. Two alkali-soluble proteins present in the electrophoretogram of mature embryos first appeared at 21 days postanthesis; most of the final profile was established by 28 days. Except for minor changes centering around the 7th week of development, the pattern from 28 days to maturity was marked by intensification of bands. The quantity of water-soluble nitrogen increased through the first 21 days of development, then declined until 42 days, when it again began to increase; it reached its highest level at maturity. There was evidence of a high peptide content 7 weeks postanthesis.

Journal Article↗
PubMed2002

A relationship between seed development, Arabinogalactan-proteins (AGPs) and the AGP mediated promotion of somatic embryogenesis.

Arabinogalactan-protein (AGP) epitopes are known to display developmentally regulated patterns of expression in several plant tissues. Therefore, AGPs have been suggested to play a role in plant development. Somatic embryogenesis is regulated by AGPs as well as by EP3 endochitinases. Using four different methods we have analysed the composition of AGPs in immature carrot seeds. The results obtained show that: (1) the native electrophoretic mobility of such AGPs changes during development; (2) AGP epitopes in immature seeds are developmentally regulated; (3) enzymatically released fragments of AGPs show that the composition of these molecules changes as a function of development; and (4) the biological activity of AGPs on the formation of somatic embryos changes depending on the age of the seeds. Our results suggest that degradation of maternally derived AGPs occurs after fertilization, while cellularization of the endosperm leads to synthesis of a new set of AGPs. The presence of an endochitinase cleavage site as well as the capacity to increase somatic embryogenesis only occurred in AGPs that were isolated from seeds in which the endosperm had been cellularized. Apparently, both EP3 endochitinases and somatic embryogenesis-promoting AGPs are developmentally regulated in immature carrot seeds.

Journal Article↗
PubMed2002

The GAMYB protein from barley interacts with the DOF transcription factor BPBF and activates endosperm-specific genes during seed development.

HvGAMYB, a MYB transcription factor previously shown to be expressed in barley aleurone cells in response to gibberellin during germination, also has an important role in gene regulation during endosperm development. The mRNA was detected early (10 DAF) in the seeds where it accumulates, not only in the aleurone layer, starchy endosperm, nucellar projection and vascular tissue, but also in the immature embryo as shown by in situ hybridization analysis. The HvGAMYB protein, expressed in bacteria, binds to oligonucleotides containing the 5'-TAACAAC-3' or 5'-CAACTAAC-3' sequences, derived from the promoter regions of the endosperm-specific genes Hor2 and Itr1, encoding a B-hordein and trypsin-inhibitor BTI-CMe, respectively. Binding is prevented when these motifs are mutated to 5'-TgACAAg-3' and 5'-CgACTgAC-3'. Transient expression experiments in co-bombarded developing endosperms demonstrate that HvGAMYB trans-activates transcription from native Hor2 and Itr1 promoters through binding to the intact motifs described above. Trans-activation of the Hor2 promoter also requires an intact prolamine box (PB). This suggests that HvGAMYB interacts in developing barley endosperms with the PB-binding factor BPBF, an endosperm-specific DOF transcriptional activator of the Hor2 gene. The in vivo interaction experiment between HvGAMYB and BPBF was done in the yeast two-hybrid system, where HvGAMYB potentiates the BPBF trans-activation capacity through interaction with its C-terminal domain.

Base Sequence↗