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.

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.

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

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 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

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.

To the item of biochemical processes at reservation and storage of milk

2018 ◽  
pp. 22-25
Author(s):  
A.D. Koval’ ◽  
◽  
A.V. Mironova ◽  
V.A. Pushkarev ◽  
K.E. Shevchenko ◽  
...  
Keyword(s):  
Biochemical Processes ◽  
And Storage

scholarly journals Expression of Mst89B and CG31287 is Needed for Effective Sperm Storage and Egg Fertilization in Drosophila

Cells ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 289
Author(s):  
Gurman Grewal ◽  
Bahar Patlar ◽  
Alberto Civetta
Keyword(s):  
Germ Line ◽  
Sperm Storage ◽  
Mature Sperm ◽  
Sperm Production ◽  
Cytogenetic Map ◽  
Egg Hatchability ◽  
Storage Organs ◽  
Competitive Success ◽  
Paternity Success ◽  
And Storage

In Drosophila, male reproductive fitness can be affected by any number of processes, ranging from development of gametes, transfer to and storage of mature sperm within the female sperm storage organs, and utilization of sperm for fertilization. We have previously identified the 89B cytogenetic map position of D. melanogaster as a hub for genes that effect male paternity success when disturbed. Here, we used RNA interference to test 11 genes that are highly expressed in the testes and located within the 89B region for their role in sperm competition and male fecundity when their expression is perturbed. Testes-specific knockdown (KD) of bor and CSN5 resulted in complete sterility, whereas KD of CG31287, Manf and Mst89B, showed a breakdown in sperm competitive success when second to mate (P2 < 0.5) and reduced fecundity in single matings. The low fecundity of Manf KD is explained by a significant reduction in the amount of mature sperm produced. KD of Mst89B and CG31287 does not affect sperm production, sperm transfer into the female bursa or storage within 30 min after mating. Instead, a significant reduction of sperm in female storage is observed 24 h after mating. Egg hatchability 24 h after mating is also drastically reduced for females mated to Mst89B or CG31287 KD males, and this reduction parallels the decrease in fecundity. We show that normal germ-line expression of Mst89B and CG31287 is needed for effective sperm usage and egg fertilization.

Periphytic microbial response to environmental phosphate bioavailability – relevance to P management in paddy fields

2021 ◽  
Author(s):  
Jianchao Zhang ◽  
Jing Su ◽  
Chao Ma ◽  
Xiangyu Hu ◽  
Henry H Teng
Keyword(s):  
Management Strategies ◽  
Phosphorus Uptake ◽  
Paddy Fields ◽  
P Availability ◽  
Biochemical Processes ◽  
Extracellular Metabolite ◽  
Microbial Response ◽  
P Utilization ◽  
Water Ecosystems ◽  
And Storage

Periphyton occurs widely in shallow-water ecosystems such as paddy fields and plays critical parts in regulating local phosphorus cycling. As such, understanding the mechanisms of the biofilm’s response to environmental P variability may lead to better perceptions of P utilization and retention in rice farms. Present study aims at exploring the biological and biochemical processes underlying periphyton’s P buffering capability through examining changes in community structure, phosphorus uptake and storage, and molecular makeup of exometabolome at different levels of P availability. Under stressed (both excessive and scarce) phosphorus conditions, we found increased populations of the bacterial genus capable of transforming orthophosphate to polyphosphate, as well as mixotrophic algae who can survive through phagotrophy. These results were corroborated by observed polyphosphate buildup under low and high P treatment. Exometabolomic analyses further revealed that periphytic organisms may substitute S-containing lipids for phospholipids, use siderophores to dissolve iron (hydr)oxides to scavenge adsorbed P, and synthesize auxins to resist phosphorus starvation. These findings not only shed light on the mechanistic insights responsible for driving the periphytic P buffer but attest to the ecological roles of periphyton in aiding plants such as rice to overcome P limitations in natural environment. Importance The ability of periphyton to buffer environmental P in shallow aquatic ecosystems may be a natural lesson on P utilization and retention in paddy fields. This work revealed the routes and tools through which periphytic organisms adapt to and regulate ambient P fluctuation. The mechanistic understanding further implicates that the biofilm may serve rice plants to alleviate P stress. Additional results from extracellular metabolite analyses suggest the dissolved periphytic exometabolome can be a valuable nutrient source for soil microbes and plants to reduce biosynthetic costs. These discoveries have the potential to improve our understanding of biogeochemical cycling of phosphorus in general and to refine P management strategies for rice farm in particular.

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