Isolation and Characterization of Two Types of Protein Bodies in the Rice Endosperm

Tanaka, Kunisuke; Sugimoto, Tsuneaki; Ogawa, Masahiro; Kasai, Zenzaburo

doi:10.1080/00021369.1980.10864167

Cited by 99 publications

(87 citation statements)

References 3 publications

(3 reference statements)

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“…We demonstrated that rice endosperm has two kinds of protein bodies, called PB-I and PB-II, in the same cell [34]. Only a single type of protein body has been reported in other cereals.…”

Section: Introductionmentioning

confidence: 94%

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cDNA cloning of an mRNA encoding a sulfur-rich 10 kDa prolamin polypeptide in rice seeds

et al. 1989

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Using a rice maturing seed pUC9 expression library, we isolated a cDNA clone corresponding to 10 kDa sulfurrich prolamin by immunoscreening. A longer cDNA clone was obtained from a λgtll library by plaque hybridization using this (32)P-labeled cDNA as a probe. A polypeptide sequence composed of 134 amino acids was deduced from the nucleotide sequence. A 24 amino acid signal peptide was assigned by computer calculation for the membrane spanning region and Edman sequencing of the purified mature polypeptide. Remarkably, 20% of methionine and 10% of cysteine were found in the mature polypeptide as well as high contents of glutamine, and hydrophobic amino acids. Part of the amino acid sequence was homologous with a conserved cysteine-rich region found in other plant prolamins. Two repeats of amino acid sequence were found in the polypeptide.

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“…We demonstrated that rice endosperm has two kinds of protein bodies, called PB-I and PB-II, in the same cell [34]. Only a single type of protein body has been reported in other cereals.…”

Section: Introductionmentioning

confidence: 94%

“…Rice prolamin polypeptides of I0, 13 and 16 kDa, located in PB-I, form a spherical concentric ring structure 1 to 2/zm in diameter [21]. The other major storage protein, glutelin, exists in PB-II, and has an ovary shape, 3 to 4 #m in diameter, with no apparent internal organization [21,31,34].…”

Section: Introductionmentioning

confidence: 99%

cDNA cloning of an mRNA encoding a sulfur-rich 10 kDa prolamin polypeptide in rice seeds

et al. 1989

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“…PB-I is generated in the ER lumen and contains prolamins, while PB-II is formed via the Golgi apparatus or by precursor accumulating vesicles from the ER that contain glutelin and a 26-kDa globulin (Krishnan et al 1986;Tanaka et al 1980;Takaiwa et al 1999;Takahashi et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Deposition of a recombinant peptide in ER-derived protein bodies by retention with cysteine-rich prolamins in transgenic rice seed

Takaiwa

Hirose

Takagi

et al. 2009

Planta

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A 7Crp peptide composed of seven major human T cell epitopes derived from the Japanese cedar pollen allergens Cry j 1 and Cry j 2 is an ideal tolerogen for peptide immunotherapy against Japanese cedar pollinosis. To maximize the accumulation level of the 7Crp peptide in transgenic rice seed, we tested endosperm specific promoters and intracellular localizations suitable for stable accumulation. A 7Crp peptide carrying the KDEL ER retention signal directed by the 2.3-kb promoter of the glutelin GluB-1, which contains a signal peptide, accumulated at the highest level of about 60 microg/grain. Notably, the 7Crp peptide predominantly accumulated in ER-derived protein bodies irrespective of the presence of various sorting signals or expression as a fusion protein with glutelin. We attribute this abnormal pattern of accumulation to the formation of disulfide bonds between the 7Crp peptide and cysteine-rich (Cys-rich) prolamin storage proteins. Furthermore, the formation of these aggregates induced the chaperone proteins BiP and PDI as an ER stress response.

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“…bumin are scanty. In contrast with glutelin and prolamine which are accumulated in protein body (PB) II and PBI of rice endosperm, respectively [36], the location of albumin and globulin in rice endosperm is unknown. At the least, major albumins are found to be nil in such protein bodies [36].…”

Section: Introductionmentioning

confidence: 99%

Gene structure and expression of rice seed allergenic proteins belonging to the ?-amylase/trypsin inhibitor family

et al. 1993

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Genomic and two novel cDNA clones for rice seed allergenic protein (RA) belonging to the alpha-amylase/trypsin inhibitor family were isolated and their nucleotide sequences determined. Ten cysteine residues deduced from nucleotide sequences were completely conserved among three cDNA clones including a clone, RA17, reported previously. One genomic clone, lambda 4, contained two RA genes, RAG1 and RAG2. Although RAG1 was cloned at the 5' portion only, two RA genes were arranged divergently. Nucleotide sequencing and DNA blotting analyses showed that RA are encoded by a multigene family consisting of at least four members. The transcriptional initiation site of RAG1 was localized at A, 26 bp upstream of the putative translational initiation codon, ATG, by the primer extension assay. The putative TATA box and CAAT box existed about 45 bp and 147 bp upstream of the transcription initiation site, respectively. A conserved sequence (ATGCAAAA) which was similar to the sequence (TGCAAAA) identified in rice glutelin promoters was observed in the 5' region of the two genes. In addition, RNA blotting analyses provided that RA genes specifically expressed in ripening seed and their transcripts accumulated maximally between 15 and 20 days after flowering.

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Isolation and Characterization of Two Types of Protein Bodies in the Rice Endosperm

Cited by 99 publications

References 3 publications

cDNA cloning of an mRNA encoding a sulfur-rich 10 kDa prolamin polypeptide in rice seeds

cDNA cloning of an mRNA encoding a sulfur-rich 10 kDa prolamin polypeptide in rice seeds

Deposition of a recombinant peptide in ER-derived protein bodies by retention with cysteine-rich prolamins in transgenic rice seed

Gene structure and expression of rice seed allergenic proteins belonging to the ?-amylase/trypsin inhibitor family

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