Ultrastructure of Mature Protein Body in the Starchy Endosperm of Dry Cereal Grain

Saito, Yuhi; Shigemitsu, Takanari; Tanaka, Kunisuke; Morita, Shigeto; Satoh, Shigeru; Masumura, Takehiro

doi:10.1271/bbb.100147

Cited by 17 publications

(19 citation statements)

References 11 publications

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“…Little is known about the maturation process of PB‐Is during seed development, because the data collected so far on maturation of PB‐Is has been limited to observations of the developing endosperm between 7 and 21 DAF. Recently, Saito et al. (2010) established a method for observation of the subcellular structures of dry rice seed after 20 DAF under high magnification by transmission electron microscopy.…”

Section: Resultsmentioning

confidence: 99%

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Formation mechanism of the internal structure of type I protein bodies in rice endosperm: relationship between the localization of prolamin species and the expression of individual genes

et al. 2012

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SUMMARYRice prolamins, a group of seed storage proteins, are synthesized on the rough endoplasmic reticulum (ER) and form type I protein bodies (PB-Is) in endosperm cells. Rice prolamins are encoded by a multigene family. In this study, the spatial accumulation patterns of various prolamin species in rice endosperm cells were investigated to determine the mechanism of formation of the internal structure of PB-Is. Immunofluorescence microscopic analysis of mature endosperm cells showed that the 10 kDa prolamin is mainly localized in the core of the PB-Is, the 13b prolamin is localized in the inner layer surrounding the core and the outermost layer, and the 13a and 16 kDa prolamins are localized in the middle layer. Real-time RT-PCR analysis showed that expression of the mRNA for 10 kDa prolamin precedes expression of 13a, 13b-1 and 16 kDa prolamin in the developing stages. mRNA expression for 13b-2 prolamin occurred after that of the other prolamin species. Immunoelectron microscopy of developing seeds showed that the 10 kDa prolamin polypeptide initially accumulates in the ER, and then 13b, 13a, 16 kDa and 13b prolamins are stacked in layers within the ER. Studies with transgenic rice seeds expressing prolamin-GFP fusion proteins under the control of native and constitutive promoters indicated that the temporal expression pattern of prolamin genes influenced the localization of prolamin proteins within the PB-Is. These findings indicate that the control of gene expression of prolamin species contributes to the internal structure of PB-Is.

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Section: Resultsmentioning

confidence: 99%

“…, 1980). PB‐Is comprise spherical, proteinaceous granules that are 1‐3 μm in diameter and have a concentric ring structure (Saito et al. , 2010).…”

Section: Introductionmentioning

confidence: 99%

Formation mechanism of the internal structure of type I protein bodies in rice endosperm: relationship between the localization of prolamin species and the expression of individual genes

et al. 2012

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“…Proteins are stored in special storage organelles generally called protein bodies (PB) in eukaryotes. The outer membrane of the PB is either single or double layered, and possess the typical lamellar structure (Jones, 1969;Morton et al, 1964;Ogawa et al, 1987;Saito et al, 2010). Remains of the lamellar protein bodies might be present in gluten and these structures can thereafter remain preserved while we separated the WG from flour through mild processing (separation) conditions.…”

Section: Nano-structural Analysismentioning

confidence: 99%

Mild gluten separation – A non-destructive approach to fine tune structure and mechanical behavior of wheat gluten films

Rasheed

Hedenqvist

Kuktaite

et al. 2015

Industrial Crops and Products

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“…Each seed sample was embedded in LR White resin (London Resin, London, UK) following the procedure of Saito et al (2010). A thin resin section (1 mm) was cut with a handmade glass knife using Ultracut UCT (Leica Microsystems, Wetzlar, Germany).…”

Section: Histochemical Analysismentioning

confidence: 99%

Protein and gene expression characteristics of a rice phosphoenolpyruvate carboxylase Osppc3; its unique role for seed cell maturation

Yamamoto

Sasou

Saito

et al. 2015

Journal of Cereal Science

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Ultrastructure of Mature Protein Body in the Starchy Endosperm of Dry Cereal Grain

Cited by 17 publications

References 11 publications

Formation mechanism of the internal structure of type I protein bodies in rice endosperm: relationship between the localization of prolamin species and the expression of individual genes

Formation mechanism of the internal structure of type I protein bodies in rice endosperm: relationship between the localization of prolamin species and the expression of individual genes

Mild gluten separation – A non-destructive approach to fine tune structure and mechanical behavior of wheat gluten films

Protein and gene expression characteristics of a rice phosphoenolpyruvate carboxylase Osppc3; its unique role for seed cell maturation

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