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

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.

Increased capacity for sucrose uptake leads to earlier onset of protein accumulation in developing pea seeds

2005 ◽  
Vol 32 (11) ◽  
pp. 997 ◽  
Author(s):  
Elke G. Rosche ◽  
Daniel Blackmore ◽  
Christina E. Offler ◽  
John W. Patrick
Keyword(s):  
Storage Protein ◽  
Protein Biosynthesis ◽  
Protein Bodies ◽  
Protein Accumulation ◽  
Sucrose Uptake ◽  
Wild Type ◽  
Protein Levels ◽  
Vicilin Gene ◽  
And Storage

Pea (Pisum sativum L.) cotyledons, overexpressing a potato sucrose transporter (StSUT1), were used to explore the hypothesis that sucrose stimulates the onset of storage protein biosynthesis. The study focused on the transition between pre-storage and storage phases of seed development. During this period supply of sucrose and hexose to transgenic cotyledons was unaffected by StSUT1 expression. However, protoplasmic levels of sucrose but not hexoses were elevated in transgenic cotyledons. Total protein levels in cotyledons followed the same temporal trend as observed for sucrose and this was reflected in an earlier appearance of protein bodies. Protein levels in wild type and StSUT1 cotyledons were found to lie on the same sucrose dose-response curve and this could be reproduced in vitro when wild type cotyledons were cultured on media containing various sucrose concentrations. Rates of [14C]sucrose uptake and incorporation into polymeric forms were consistent with protoplasmic sucrose supplying a proportion of the carbon skeletons required for storage protein accumulation. In addition, vicilin gene expression was up-regulated earlier in StSUT1 cotyledons. We conclude that sucrose functions both as a signal and fuel to stimulate storage protein accumulation and assembly into protein bodies. An earlier stimulation of storage protein synthesis is considered to largely account for the 14% increase in protein levels of StSUT1 seeds at harvest.

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.

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.

scholarly journals The 2-oxoglutarate/malate translocator mediates amino acid and storage protein biosynthesis in pea embryos

2009 ◽  
Vol 61 (2) ◽  
pp. 350-363 ◽  
Author(s):  
Erik Riebeseel ◽  
Rainer E. Häusler ◽  
Ruslana Radchuk ◽  
Tobias Meitzel ◽  
Mohammad-Reza Hajirezaei ◽  
...  
Keyword(s):  
Amino Acid ◽  
Storage Protein ◽  
Protein Biosynthesis ◽  
And Storage

scholarly journals Inheritance and mapping of vicilin storage protein genes in Pisum Sativum L

Heredity ◽  
1984 ◽  
Vol 53 (1) ◽  
pp. 185-191 ◽  
Author(s):  
Sayed H Mahmoud ◽  
John A Gatehouse
Keyword(s):  
Pisum Sativum ◽  
Storage Protein ◽  
Pisum Sativum L ◽  
Storage Protein Genes

The Carbohydrate of Storage Glycoproteins From Seeds of Pisum sativum: Characterization and Distribution on Component Polypeptides

1979 ◽  
Vol 6 (4) ◽  
pp. 435 ◽  
Author(s):  
RA Davey ◽  
WF Dudman
Keyword(s):  
Pisum Sativum ◽  
Storage Proteins ◽  
Protein Biosynthesis ◽  
Similar Amount ◽  
Carbohydrate Composition ◽  
Con A ◽  
Major Site ◽  
Unbound Fraction ◽  
Sepharose 4B ◽  
Mature Seeds

Storage proteins were extracted from isolated protein bodies from mature seeds of Pisum sativum and separated into one legumin and four vicilin fractions. A comparative study was made of the glycosylation of each fraction and all were found to contain covalently attached carbohydrate at a level of between 0.9 and 1.4% of the protein weight. The carbohydrate composition of the legumin fraction was different from that of the vicilin fractions: the major sugar in legumin was glucose (Glc) with some mannose (Man) and glucosamine (GlcN) while, for all vicilin fractions, Man was the major sugar wlth GlcN, Glc and galactose (Gal) in lesser amounts. There were minor differences in carbohydrate composition between vicilin fractions. Each of the vicilin fractions was further separated by concanavalin A (Con A)-Sepharose 4B chromatography into two fractions. The protein which bound to Con A always contained more carbohydrate than the unbound fraction and, in one vicilin fraction, the unbound protein was not glycosylated. No legumin bound to Con A. Both the 20 and 40 kdalton polypeptides of legumin are glycosylated while the 14 kdalton polypeptide was the major site of glycosylation for all vicilin fractions. One vicilin fraction also has a similar amount of carbohydrate associated with a 50 kdalton polypeptide. Some other polypeptides in the vicilins were glycosylated but to a much lesser extent. These findings are compared to those for other legume storage proteins and their significance in storage protein biosynthesis is discussed.

Germination and Storage of Pea (Pisum sativum L.) Pollen 1

1956 ◽  
Vol 48 (8) ◽  
pp. 347-352 ◽  
Author(s):  
Stephen J. Warnock ◽  
D. J. Hagedorn
Keyword(s):  
Pisum Sativum ◽  
Pisum Sativum L ◽  
And Storage
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