Dual Regulated RNA Transport Pathways to the Cortical Region in Developing Rice Endosperm

Hamada, Shigeki; Ishiyama, Keiki; Sakulsingharoj, Chotipa; Choi, Sang Bong; Wu, Yujia; Wang, Changlin; Singh, S. S.; Kawai, Nobuyoshi; Messing, Joachim; Okita, Thomas W.

doi:10.1105/tpc.013821

Cited by 73 publications

(115 citation statements)

References 40 publications

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“…Ongoing studies in this laboratory indicate the existence of multiple RNA transport pathways from the nucleus to the cortical region in developing rice endosperm cells (Hamada et al, 2003). In addition to the prolamine RNA pathway to the PB-ER, there exists a glutelin RNA pathway as well as a constitutive pathway to the cisternal ER.…”

Section: Discussionmentioning

confidence: 93%

“…The formation of the particle is likely to involve generalized localization elements that direct transport to the cortical ER and specialized signal determinants (zip codes) that target the RNA to specific subdomains of the cortical ER. These specialized cis elements or zip codes have been identified for the prolamine RNA and are sufficient to direct reporter RNAs to the PB-ER (Hamada et al, 2003). The glutelin 3Ј untranslated region also has one or more specialized cis elements to direct the RNA to the cortical ER (Choi et al, 2000;Hamada et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

“…Prolamines are sequestered within the ER lumen as intracisternal granules, whereas glutelins are transported via the Golgi to storage vacuoles. We demonstrated previously that the rice storage protein RNAs are localized to distinct subdomains of the ER Choi et al, 2000;Hamada et al, 2003). Glutelin RNAs, which code for the major storage protein, are localized to the cisternal ER, whereas prolamine RNAs are targeted to ER that surrounds the intracisternal prolamine protein bodies (PB-ER).…”

Section: Introductionmentioning

confidence: 99%

“…Results obtained from deletion studies of prolamine RNA indicate that PB-ER targeting requires the presence of two cis elements (Hamada et al, 2003) or "zip codes" (Singer, 1993). The presence of a single zip code results in localization not only to the PB-ER but also to the cisternal ER.…”

Section: Introductionmentioning

confidence: 99%

“…These observations indicate that prolamine RNAs are directed to the PB-ER and that the absence of one or more zip codes results in RNAs transported along a default pathway to the cisternal ER. Interestingly, despite the existence of this constitutive RNA transport to the cisternal ER, glutelin RNAs are localized to the cisternal ER by a regulated pathway whose RNA signal determinant apparently is dominant over the zip codes that direct prolamine RNA to the PB-ER (Choi et al, 2000;Hamada et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

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The Transport of Prolamine RNAs to Prolamine Protein Bodies in Living Rice Endosperm Cells[W]

et al. 2003

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RNAs that code for the major rice storage proteins are localized to specific subdomains of the cortical endoplasmic reticulum (ER) in developing endosperm. Prolamine RNAs are localized to the ER and delimit the prolamine intracisternal inclusion granules (PB-ER), whereas glutelin RNAs are targeted to the cisternal ER. To study the transport of prolamine RNAs to the surface of the prolamine protein bodies in living endosperm cells, we adapted a two-gene system consisting of green fluorescent protein (GFP) fused to the viral RNA binding protein MS2 and a hybrid prolamine RNA containing tandem MS2 RNA binding sites. Using laser scanning confocal microscopy, we show that the GFP-labeled prolamine RNAs are transported as particles that move at an average speed of 0.3 to 0.4 m/s. These prolamine RNA transport particles generally move unidirectionally in a stop-and-go manner, although nonlinear bidirectional, restricted, and nearly random movement patterns also were observed. Transport is dependent on intact microfilaments, because particle movement is inhibited rapidly by the actin filament-disrupting drugs cytochalasin D and latrunculin B. Direct evidence was obtained that these prolamine RNA-containing particles are transported to the prolamine protein bodies. The significance of these results with regard to protein synthesis in plants is discussed.

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Section: Discussionmentioning

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The Transport of Prolamine RNAs to Prolamine Protein Bodies in Living Rice Endosperm Cells[W]

et al. 2003

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Embryonic expression of type XIX collagen is transient and confined to muscle cells

et al. 2001

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Plants have been used to produce many diverse and valuable recombinant proteins, including subunit vaccines, antibodies and antibody fragments, hormones, blood products, cytokines, and enzymes. Different plant species and platforms have been explored as production hosts, each with unique properties in terms of the gene transfer method, production time, environmental containment, scalability, downstream processing strategy, protein folding and accumulation, and overall costs. Seed‐based systems have many advantages because they exploit the natural storage properties of seeds, which facilitate batch processing and distribution. Seeds possess specialized storage organelles that may be used to accumulate recombinant proteins, offering stability both in planta and after harvest in the final preparation/formulation. The post‐harvest stabilizing effect of seeds allows recombinant subunit vaccines and antibodies to be delivered via the mucosal route because they are better able to withstand this harsh microenvironment when protected by the plant matrix. Native storage organelles such as starch granules and protein bodies offer this protective effect, but protein storage organelles can also be induced ectopically in vegetative tissues. In this paper, we discuss the technical capabilities of storage organelle‐based expression platforms and their potential applications.

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Using storage organelles for the accumulation and encapsulation of recombinant proteins

Khan

Twyman

Arcalís

et al. 2012

Biotechnology Journal

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Plants have been used to produce many diverse and valuable recombinant proteins, including subunit vaccines, antibodies and antibody fragments, hormones, blood products, cytokines, and enzymes. Different plant species and platforms have been explored as production hosts, each with unique properties in terms of the gene transfer method, production time, environmental containment, scalability, downstream processing strategy, protein folding and accumulation, and overall costs. Seed-based systems have many advantages because they exploit the natural storage properties of seeds, which facilitate batch processing and distribution. Seeds possess specialized storage organelles that may be used to accumulate recombinant proteins, offering stability both in planta and after harvest in the final preparation/formulation. The post-harvest stabilizing effect of seeds allows recombinant subunit vaccines and antibodies to be delivered via the mucosal route because they are better able to withstand this harsh microenvironment when protected by the plant matrix. Native storage organelles such as starch granules and protein bodies offer this protective effect, but protein storage organelles can also be induced ectopically in vegetative tissues. In this paper, we discuss the technical capabilities of storage organelle-based expression platforms and their potential applications.

show abstract

Dual Regulated RNA Transport Pathways to the Cortical Region in Developing Rice Endosperm

Cited by 73 publications

References 40 publications

The Transport of Prolamine RNAs to Prolamine Protein Bodies in Living Rice Endosperm Cells[W]

The Transport of Prolamine RNAs to Prolamine Protein Bodies in Living Rice Endosperm Cells[W]

Embryonic expression of type XIX collagen is transient and confined to muscle cells

Using storage organelles for the accumulation and encapsulation of recombinant proteins

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