scholarly journals Genetically Controlled Electrophoretic Variants of a Storage Protein in Pisum Sativum

1968 ◽  
Vol 21 (4) ◽  
pp. 827 ◽  
Author(s):  
MJ Hynes
Keyword(s):  
Pisum Sativum ◽  
Genetic Control ◽  
Storage Protein ◽  
Storage Proteins ◽  
Genetic Studies ◽  
Electrophoretic Variants ◽  
Electrophoretic Patterns ◽  
Wheat Storage Proteins ◽  
And Storage

A number of electrophoretic variants of plant enzymes have been described and the genetic control of these variants determined (e.g. Beckman, Scandalios, and Brewbaker 1964; Schwartz 1964; Scandalios 1965). However, little work has been done on structural and storage proteins of plants. Varietal differences have been observed in the electrophoretic patterns of wheat storage proteins (Graham and Morton 1963) and two forms of arachin, a storage protein of the peanut, have been described (Tombs 1964), though no genetic studies of these differences have been made. This communication describes the detection and the partial characterization of variants of proteins extracted from the cotyledons of Pisum sativum seeds and some preliminary breeding tests to determine their genetic control.

scholarly journals The characterization of cDNA clones coding for wheat storage proteins

1983 ◽  
Vol 11 (10) ◽  
pp. 2961-2977 ◽  
Author(s):  
Dorothea Bartels ◽  
Richard D. Thompson
Keyword(s):  
Storage Proteins ◽  
Cdna Clones ◽  
Wheat Storage Proteins

Amino acid transporter expression and localisation studies in pea (Pisum sativum)

2007 ◽  
Vol 34 (11) ◽  
pp. 1019 ◽  
Author(s):  
Mechthild Tegeder ◽  
Qiumin Tan ◽  
Aleel K. Grennan ◽  
John W. Patrick
Keyword(s):  
Amino Acid ◽  
Pisum Sativum ◽  
Storage Protein ◽  
Expression Patterns ◽  
Phloem Loading ◽  
Transfer Cells ◽  
Protein Accumulation ◽  
Developmentally Regulated ◽  
And Storage ◽  
Seed Coats

Expression of the amino acid permeases PsAAP1 and PsAAP2 was analysed in developing pea (Pisum sativum L.) plants. Both transporters were expressed in seed coats and cotyledon epidermal transfer cells and storage parenchyma cells. AAP expression is developmentally regulated and coincides with the onset of storage protein synthesis. Nitrogen was shown to induce AAP expression and AAP transcript levels were upregulated during the photoperiod. Analysis of Arabidopsis thaliana AAP1 promoter activity in pea, using promoter-β-glucuronidase (promotor-GUS) studies, revealed targeting of GUS to seed coats and cotyledon epidermal transfer cells. Expression was found in the nutritious endosperm during the early stages of seed development, whereas GUS staining in embryos was detected from the heart stage onward. In addition, AAP1 expression was observed in the phloem throughout the plant. This finding equally applied to PsAAP1 expression as shown by in situ mRNA hybridisation, which also demonstrated that PsAAP1 expression was localised to companion cells. Overall, PsAAP1 expression patterns and cellular localisation point to a function of the transporter in phloem loading of amino acids for translocation to sinks and in seed loading for development and storage protein accumulation.

Cotyledonary Storage Proteins in Pisum Sativum. II. Hereditary Variation in Components of the Legumin and Vicilin Fractions

1978 ◽  
Vol 5 (3) ◽  
pp. 281 ◽  
Author(s):  
JA Thomson ◽  
HE Schroeder
Keyword(s):  
Pisum Sativum ◽  
Phenotypic Variation ◽  
Storage Protein ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Gene Products ◽  
Hereditary Variation ◽  
Pea Seeds ◽  
Parental Lines ◽  
Variant System

Gel electrophoresis has been used to investigate genetically controlled variation in storage-protein constituents forming five series of bands (LA-LE) derived from legumin fractions, and three series of bands (VA-VC) from vicilin fractions, of pea seeds. In each variant system, the phenotypes of the storage-protein polypeptides from F1 seeds were additive with respect to the band patterns of the parental lines, and identical in reciprocal crosses. Neither dominance nor formation of new interaction products was observed. Variation in the three systems involving vicilin polypeptides and two of those involving legumin components was found to be based on allelic alternatives at single loci designated Vicilin A (Vca), Vicilin B (Vcb), Vicilin C (Vcc), Legumin A (Lga) and Legumin C (Lgc). For each of these variant systems, the gene products involved and the basis of the phenotypic variation have been discussed. Variants of the VC band complex, in which mobility of two bands both composed of 12 and 14 kdalton polypeptides is altered, appear likely to correspond to vicilin variants described previously. Type lines are specified for each of the variant phenotypes analysed, and for the genes designated.

Time Course of Lectin and Storage Protein Biosynthesis in Developing Pea (Pisum sativum) Seeds

1993 ◽  
Vol 374 (7-12) ◽  
pp. 887-894 ◽  
Author(s):  
Mathias WENZEL ◽  
Heinrich GERS-BARLAG ◽  
Anneliese SCHIMPL ◽  
Harold RÜDIGER
Keyword(s):  
Pisum Sativum ◽  
Storage Protein ◽  
Time Course ◽  
Protein Biosynthesis ◽  
And Storage

The conversion of carbon and nitrogen into starch and storage proteins in developing storage organs: an overview

2000 ◽  
Vol 27 (6) ◽  
pp. 561 ◽  
Author(s):  
I. Halil Kavakli ◽  
Casey J. Slattery ◽  
Hiroyuki Ito ◽  
Thomas W. Okita
Keyword(s):  
Storage Protein ◽  
Storage Proteins ◽  
Protein Biosynthesis ◽  
Biochemical Processes ◽  
Normal Site ◽  
Enzyme Isoforms ◽  
Storage Organs ◽  
Recent Developments ◽  
Starch Mutants ◽  
And Storage

In this article we provide an overview on recent developments in starch and storage protein biosynthesis, two seemingly distinct biochemical processes, which have been shown to be inter-dependent based on results from genetic and transgenic studies. The pathway of carbon to starch in cereal seeds has been found to be substantially different from other plants in having ADPglucose, the precursor of starch biosynthesis, formed mainly in the cyto-plasm in addition to the normal site of synthesis, the plastid. Analysis of starch mutants and the use of antisense technology have shed considerable light on the possible roles of individual starch synthase and branching enzyme isoforms as well as those of enzyme activities normally associated with a degradative function in starch formation. Analysis of storage protein in the model system rice indicates that sites of protein synthesis and compartmentation of macromolecules are stratified within specific intracellular regions. The possible implications of this intracellular partitioning of carbon (starch) and nitrogen (storage protein) utilization are discussed.

Comparisons between the roles of the fruit tissues, osmoticum and abscisic acid in maintaining tomato seed development and storage protein synthesis

1993 ◽  
Vol 3 (1) ◽  
pp. 25-34 ◽  
Author(s):  
Tannis Berry ◽  
J. Derek Bewley
Keyword(s):  
Protein Synthesis ◽  
Abscisic Acid ◽  
Storage Protein ◽  
Storage Proteins ◽  
Tomato Seed ◽  
Intimate Contact ◽  
Developing Seed ◽  
Mannanase Activity ◽  
And Storage

AbstractFive distinct groups of storage proteins are synthesized by embryos during development in the fruit at 35 days after pollination (35 DAP); none of them is synthesized in germinating embryos 48 h after isolation (48 HASI) of the seeds from the fruit. Endo-β-mannanase, a marker of germination and seedling growth, is produced in the isolated seeds, but not in the developing seed in situ 35 DAP. When seeds at this stage are removed from the fruit, but remain in intimate contact with the locular and sheath tissue, they continue to synthesize storage proteins for at least 48 HASI. Removal of the sheath from seeds isolated 35 DAP stops storage protein synthesis, and increases endo-β-mannanase activity. Both abscisic acid (ABA) and osmoticum at physiological concentrations maintain the synthesis of storage proteins in seeds isolated 35 DAP for at least 48 HASI, although osmoticum is more effective in preventing their eventual germination. Thus the effects of the sheath and the locular tissue are mimicked by both ABA and osmoticum in relation to the maintenance of storage protein synthesis in seeds 35 DAP and in the suppression of endo-β-mannanase activity for at least 48 HASI.

scholarly journals The purification and characterization of a third storage protein (convicilin) from the seeds of pea (Pisum sativum L.)

1980 ◽  
Vol 191 (2) ◽  
pp. 509-516 ◽  
Author(s):  
R R Croy ◽  
J A Gatehouse ◽  
M Tyler ◽  
D Boulter
Keyword(s):  
Genetic Variation ◽  
Pisum Sativum ◽  
Storage Protein ◽  
Purification And Characterization ◽  
Native Form ◽  
Pisum Sativum L ◽  
A Subunit ◽  
Cnbr Cleavage ◽  
Pea Seeds

A third storage protein, distinct from legumin and vicilin, has been purified from the seeds of pea (Pisum sativum L.). This protein has been named ‘convicilin’ and is present in protein bodies isolated from pea seeds. Convicilin has a subunit mol.wt. of 71 000 and a mol.wt. in its native form of 290 000. Convicilin is antigenically dissimilar to legumin, but gives a reaction of identity with vicilin when tested against antibodies raised against both proteins. However, convicilin contains no vicilin subunits and may be clearly separated from vicilin by non-dissociating techniques. Unlike vicilin, convicilin does not interact with concanavalin A, and contains insignificant amounts of carbohydrates. Limited heterogeneity, as shown by isoelectric focusing, N-terminal analysis, and CNBr cleavage, is present in convicilin isolated from a single pea variety; genetic variation of the protein between pea lines has also been observed.

Electrophoretic and immunochemical techniques for the molecular reassessment of relationships within Vicieae

2007 ◽  
Vol 55 (2) ◽  
pp. 131-147
Author(s):  
R. Sammour
Keyword(s):  
Pisum Sativum ◽  
Vicia Faba ◽  
Cicer Arietinum ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Immunochemical Study ◽  
Partial Identity ◽  
Electrophoretic Patterns ◽  
Immunochemical Techniques

In this study, an array of electrophoretic and immunochemical techniques was used to investigate the legumins, vicilins and albumins of seed storage proteins in Pisum sativum , Vicia faba , Lens esculentum , and Cicer arietinum to delimit the boundary of the tribe Vicieae and to clarify the systematic position of the genus Cicer . The band patterns of the legumins of these species were broadly similar in that they had bands at Mr 60 kDa which disappeared in the presence of 2-mercaptoethanol, giving rise to two sets of new bands, at Mr approximately 40 kDa and 20 kDa, representing acidic or α and basic or β subunits. The band patterns of the vicilins were also quite similar in that they showed bands at Mr approximately 71 kDa (convicilin) and 50 kDa (vicilin), which were not altered by the presence of 2-mercaptoethanol. Serologically, the legumins of Vicia faba and Lens esculentum exhibited total identity with Pisum legumin antiserum under nonreducing conditions, whereas the legumin of Cicer arietinum exhibited only partial identity, which was attributed to the failure of the low molecular subunit pair (Mr 33 kDa) to react with Pisum legumin antiserum. On the other hand, the vicilins of Vicia faba , Lens esculentum and Cicer arietinum had only partial identity with the vicilin of Pisum sativum , which was due to the failure of a number of subunits along the electrophoretic patterns of these species to react with Pisum sativum vicilin antiserum. The electrophoretic patterns of Vicia faba , Lens esculentum and Cicer arietinum were markedly different for the albumins. However, immunochemically they gave a positive reaction with Pisum major albumin antiserum (Mr 25 kDa) and showed a band with a molecular weight slightly higher than the major albumin of Pisum sativum . Extending the immunochemical study to members of the Phaseoleae, Glycineae, Cajaneae and Diocleae revealed that the vicilin and legumin of Cicer were more closely related to the Vicieae than to these tribes. Thus the data presented in this work recommended the classification of Cicer under Vicieae rather than as a separate tribe Cicerideae .

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