Rice Mutant Lines Lacking .ALPHA.-Globulin.

Iida, Shūichi; Miyahara, Kosuke; Nishio, Takeshi

doi:10.1270/jsbbs1951.48.45

Cited by 20 publications

(23 citation statements)

References 14 publications

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“…1B). The 32 kDa polypeptide, which belongs to the glutelin fraction (Iida et al 1998), was detected at 10 DAF and accumulated in parallel with other glutelin polypeptides in K × 433 and LGC-Jun (Fig. 1A).…”

Section: Resultsmentioning

confidence: 97%

“…There is a 3.5 kb deletion between two highly similar glutelin genes at the Lgc1 locus, which forms a double-stranded RNA molecule and induces RNA silencing, and the high prolamin content of LGC1 is considered to be compensating for the reduced glutelin content (Kusaba et al 2003). K × 433 is derived from a backcross of Koshihikari and the mutant line 89WPKG30-433 (Ashida et al 2006, Iida et al 1998 and shows the lack of a 26 kDa globulin, which is controlled by a single recessive gene, glb1. Morita et al (2007) reported that the glb1 mutant has a 63 kb deletion in a region including the 26 kDa globulin gene.…”

Section: Introductionmentioning

confidence: 99%

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Ultrastructure of protein bodies in mutant rice (Oryza sativa L.) with altered storage protein composition

et al. 2011

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Many rice mutants with altered storage protein composition, which relate to protein body II (PB-II), have been produced in order to obtain rice with new cooking properties or lowered protein digestibility, but the PB structures in the endosperm of such mutants remain obscure. We examined the polypeptide composition and ultrastructure of the endosperm during seed development using rice mutants with the low-glutelin-content gene (Lgc1) and/or 26 kDa globulin deficient gene (glb1). Lgc1 and glb1 have deletions of a region including glutelin structural genes and 26 kDa globulin gene, respectively. Mutants with Lgc1 accumulated prolamin polypeptides from an early stage of seed development, and numerous intact PB-I and a few, small, chipped PB-II were observed in the endosperm. The glb1 mutant showed deformed PB-II structures, which had similar electron density to wild-type PB-II. Both glutelins and globulins accumulate in PB-II, but the influence of the change in their composition on PB-II structure would be different. The unique PB-II structure in the glb1 mutant may bring about new processing properties for rice.

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Section: Resultsmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Ultrastructure of protein bodies in mutant rice (Oryza sativa L.) with altered storage protein composition

et al. 2011

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“…Although LGC-1 and LGCsoft also have the low-glutelin characteristic, the ratio of glutelins to total protein was higher than that in LGC-Katsu. It is not elucidated why the low-glutelin characteristic appears so dominantly in LGC-Katsu, which has a low-glutelin gene Lgc1 (Iida et al, 1993a(Iida et al, , 1993b, as in LGC-1 and LGCsoft, and also has 26-kDa-globulindefi cient gene glb1 (Iida et al, 1998). In addition, the glb1 function is not elucidated.…”

Section: Discussionmentioning

confidence: 99%

Analysis of Storage Protein Distribution in Rice Grain of Seed-Protein Mutant Cultivars by Immunofluorescence Microscopy

Ohdaira

Masumura

Nakatsuka

et al. 2011

Plant Production Science

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“…In the low-glutelin rice LGC1, the content of prolamin increased, while the content of glutelin decreased (Iida et al 1993(Iida et al , 1998. In sake brewing, proteins in rice seed are an important factor imparting the sake flavor, but too much protein produces an undesirable flavor.…”

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confidence: 99%

Ultrastructure of low-glutelin rice endosperm

Furukawa

Itou

Masumura

et al. 2007

Plant Biotechnology

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Low-glutelin rice has low content of digestible protein glutelin, and is expected to use as raw material for sake brewing. To characterize endosperm cell structure of low-glutelin rice, the storage proteins of endosperm cells in polished rice (degree of milling, 70%; used as raw material for sake brewing) of two low-glutelin rice varieties, LGC1 and Tashu-kei 1001, and two general rice cultivars (brewer's rice), Hyogokitanishiki and Yamadanishiki, were observed using a transmission electron microscope. Low-glutelin rice differed from general rice cultivars in the composition of major storage proteins and the transgranular distribution of storage proteins as well as in the distribution of protein bodies in endosperm cells. Furthermore, low-glutelin rice had a specific endosperm cell structure containing many type I protein bodies even in the outer layer of polished rice grains.

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Rice Mutant Lines Lacking .ALPHA.-Globulin.

Cited by 20 publications

References 14 publications

Ultrastructure of protein bodies in mutant rice (Oryza sativa L.) with altered storage protein composition

Ultrastructure of protein bodies in mutant rice (Oryza sativa L.) with altered storage protein composition

Analysis of Storage Protein Distribution in Rice Grain of Seed-Protein Mutant Cultivars by Immunofluorescence Microscopy

Ultrastructure of low-glutelin rice endosperm

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