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Manipulation of starch and storage p...

Sakulsingharoj, Chotipa.

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Manipulation of starch and storage protein synthesis in rice seeds.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Manipulation of starch and storage protein synthesis in rice seeds./
Author:	Sakulsingharoj, Chotipa.
Description:	105 p.
Notes:	Source: Dissertation Abstracts International, Volume: 63-07, Section: B, page: 3161.
Contained By:	Dissertation Abstracts International63-07B.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3058815
ISBN:	0493744126

Manipulation of starch and storage protein synthesis in rice seeds.
Sakulsingharoj, Chotipa.

Manipulation of starch and storage protein synthesis in rice seeds. - 105 p.

Source: Dissertation Abstracts International, Volume: 63-07, Section: B, page: 3161.

Thesis (Ph.D.)--Washington State University, 2002.

Starch and storage protein syntheses are inter-related processes in cereals. Although much information is known on the biosynthesis of these macromolecules, the basis for this relationship remains unknown. The studies described here were designed to increase our understanding of the molecular and cellular processes of starch and storage protein and to provide insight into the molecular basis for their relationship. The quantity of starch in cereal grains is controlled by the regulatory enzyme ADP-glucose pyrophosphorylase (AGPase). Manipulation of AGPase expression during rice seed development was performed to increase starch synthesis, sink strength and, in turn, seed weight. The Escherichia coli triple mutant AGPase, which is insensitive to allosteric effectors, was introduced into rice seeds by Agrobacterium-mediated transformation. The mutated enzyme was expressed in the cytosol or amyloplast of endosperm cells to determine whether the intracellular sites of ADP-glucose formation affected starch synthesis. The results indicate that starch synthesis and consequently seed weight can be increased by manipulating AGPase activity levels present in the cytosol but not in the amyloplast of transgenic rice seeds. In addition to accumulation of starch, rice seeds store two types of storage proteins, prolamines and glutelins, in separate compartments of endosperm cells. It has been proposed that the targeting of these proteins to different compartments is facilitated by their RNA localization. To investigate whether mRNA localization affected storage protein targeting and accumulation in rice endosperm cells, transgenic rice plants expressing different maize delta-zein RNAs were analyzed using in situ RT-PCR and confocal microscopy. The results indicate that delta-zein mRNA is localized on the endoplasmic reticulum membrane of the prolamine protein body and that the signal peptide RNA coding sequence is essential for delta-zein RNA localization. Immunocytochemical analysis at the electron microscopy level reveals that maize delta-zein accumulates exclusively within the prolamine protein bodies. These observations support the hypothesis that delta-zein mRNA localization facilitates the targeting and deposition of delta-zein protein in rice prolamine protein bodies. Overall, the results of the studies described here have increased our understanding of starch and protein syntheses, information that will be useful for the genetic improvement of cereal grains.

ISBN: 0493744126Subjects--Topical Terms:

1017719
Biology, Molecular.

Manipulation of starch and storage protein synthesis in rice seeds.
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500 $a Chair: Thomas W. Okita.
502 $a Thesis (Ph.D.)--Washington State University, 2002.
520 $a Starch and storage protein syntheses are inter-related processes in cereals. Although much information is known on the biosynthesis of these macromolecules, the basis for this relationship remains unknown. The studies described here were designed to increase our understanding of the molecular and cellular processes of starch and storage protein and to provide insight into the molecular basis for their relationship. The quantity of starch in cereal grains is controlled by the regulatory enzyme ADP-glucose pyrophosphorylase (AGPase). Manipulation of AGPase expression during rice seed development was performed to increase starch synthesis, sink strength and, in turn, seed weight. The Escherichia coli triple mutant AGPase, which is insensitive to allosteric effectors, was introduced into rice seeds by Agrobacterium-mediated transformation. The mutated enzyme was expressed in the cytosol or amyloplast of endosperm cells to determine whether the intracellular sites of ADP-glucose formation affected starch synthesis. The results indicate that starch synthesis and consequently seed weight can be increased by manipulating AGPase activity levels present in the cytosol but not in the amyloplast of transgenic rice seeds. In addition to accumulation of starch, rice seeds store two types of storage proteins, prolamines and glutelins, in separate compartments of endosperm cells. It has been proposed that the targeting of these proteins to different compartments is facilitated by their RNA localization. To investigate whether mRNA localization affected storage protein targeting and accumulation in rice endosperm cells, transgenic rice plants expressing different maize delta-zein RNAs were analyzed using in situ RT-PCR and confocal microscopy. The results indicate that delta-zein mRNA is localized on the endoplasmic reticulum membrane of the prolamine protein body and that the signal peptide RNA coding sequence is essential for delta-zein RNA localization. Immunocytochemical analysis at the electron microscopy level reveals that maize delta-zein accumulates exclusively within the prolamine protein bodies. These observations support the hypothesis that delta-zein mRNA localization facilitates the targeting and deposition of delta-zein protein in rice prolamine protein bodies. Overall, the results of the studies described here have increased our understanding of starch and protein syntheses, information that will be useful for the genetic improvement of cereal grains.
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