The structure of rice storage protein glutelin precursor deduced from cDNA

Takaiwa, Fumio; Kikuchi, Shoshi; Oono, Kiyoharu

doi:10.1016/0014-5793(86)81335-7

Cited by 59 publications

(28 citation statements)

References 12 publications

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“…In this analysis, globulin mRNA was detectable by 3 Our analysis showed that the amino acid sequence specified by pOG2 is 70% identical to that of the rice globulin (glutelin) reported by Takaiwa et aL (27) (Fig. 5, right).…”

Section: Resultssupporting

confidence: 74%

“…6B) and the rice globulin (glutelin) (Fig. 6C) The oat globulin sequence is from cDNA clone pOG2, the soybean glycinin sequence is from the Gy2 gene (18), and the rice globulin (glutelin) sequence is from cDNA clone pREE6 1 (27). The sequences were aligned using the Microgenie computer program which inserts gaps to maximize homology.…”

Section: Resultsmentioning

confidence: 99%

“…This arrangement suggests that regions containing these conserved proline residues are important in the folding of the acidic polypeptide around the basic polypeptide and that considerable sequence divergence is tolerated in other regions of the acidic chain. Gy2 (18), the oat sequence (B) is from cDNA clone pOG2, and the rice sequence (C) is from cDNA clone pREE61 (27). The arrow indicates the position of the hypervariable region, which falls roughly between residues 270 and 310.…”

Section: Resultsmentioning

confidence: 99%

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Molecular Characterization of Oat Seed Globulins

Shotwell

Afonso²,

Davies³

et al. 1988

Plant Physiol.

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We have isolated full-length cDNA clones that encode oat (Avena sativa) seed storage globulin mRNAs from a cDNA library in the expression vector lambda gtll. The longest of these clones, pOG2, has an 1840-base pair insert that encodes a complete precursor subunit with a signal peptide of 24 amino acids followed by an acidic polypeptide of 293 amino acids and a basic polypeptide of 201 amino acids. Near the C terminus of the acidic polypeptide are four repeats of a higly conserved, glutamine-rich octapeptide. Other oat globulin cDNA clones contain five of these repeats. Nucleotide sequence comparisons between these clones indicate that the genes encoding these proteins are highly conserved. We estimate there to be 7 to 10 genes for the oat globulin per haploid genome. Comparisons of amino acid sequences show that the oat globulin is 30 to 40% homologous with storage globulins of legumes and about 70% homologous with the rice seed storage globulin (glutelin).During their development, plant seeds accumulate large amounts of storage proteins that serve as sources of nitrogen, sulfur, and carbon compounds during seed germination (25). Two major classes of storage proteins can be distinguished: globulins, which are found principally in the cotyledons and axis of the embryo, and prolamines, which are found in the endosperm of cereal seeds (13). Two major types of storage globulins have been described that have sedimentation coefficients ofabout 7S and 11S. The proportion of the two types of globulins is variable among dicots; monocot embryos contain only the 7S globulin, which is present in the scutellum.Storage globulins account for most of the protein in dicot seeds, but they generally make up only a small fraction of the protein found in cereal seeds. Instead, most cereals contain predominantly prolamine-type storage proteins. Oats and rice are exceptions. These two contain only small amounts ofprolamine (5-10%), and most of their storage protein is an 11 to 12S globulin that is synthesized in the endosperm. Both of these proteins are structurally related to the 11S globulins found in dicots (25), but both are much less soluble than the dicot 11S globulins. The oat globulin requires 0.8 to 1.0 M NaCl for solubility, whereas the characteristics of the rice globulin (glutelin) are such that denaturing solvents are required for solvation.Previous studies in our laboratory (29) and elsewhere (5, 7)

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Section: Resultssupporting

confidence: 74%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Molecular Characterization of Oat Seed Globulins

Shotwell

Afonso²,

Davies³

et al. 1988

Plant Physiol.

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“…These results indicated that the subunit composition of the 64-kD glutelin is different from those of high molecular mass and that the high-molecular-mass glutelins were polymers of the 130-kD protein. This observation is coincident with the reports that different nucleotide sequences of rice glutelin cDNA were found 8,9) and that the protein is encoded in different gene subfamilies. 10 ,11) The 64-kD glutelin does not polymerize as 130-kD glutelin does to form high-molecular-mass glutelin by intermolecular disulfide bridges in the protein body (PB-II).…”

supporting

confidence: 90%

Heterogeneity in Subunit Composition of Glutelin in Rice Protein Bodies

Sugimoto

Tanaka

Kasai

1991

Agricultural and Biological Chemistry

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“…The 5 bp deletion caused a frame-shift of the PLA1 gene. The single-base Glutinous endosperm WX (Os06g0133000) Wang et al (1990) Shortened plastochron PLA1 (Os10g0403000) Miyoshi et al (2004) Shortened plastochron PLA2 (Os01g0907900) Kawakatsu et al (2006) Gibberellin deficiency CPS (Os02g0278700) Sakamoto et al (2004) Gibberellin deficiency KAO (Os06g0110000) Sakamoto et al (2004) Gibberellin deficiency GA3ox2 (Os01g0177400) Itoh et al (2001) Gibberellin insensitivity GID1 (Os05g0407500) Ueguchi-Tanaka et al (2005) Gibberellin insensitivity GID2 (Os02g0580300) Sasaki et al (2003) Glutelin deficiency GluA1 (Os01g0762500) Takaiwa et al (1986) Glutelin deficiency GluA2 (Os10g0400200) Takaiwa et al (1987) Glutelin deficiency GluB4/B5 (Os02g0268300/Os02g0268100) Masumura et al (1989) α-Globulin deficiency α-globulin (Os05g0499100) Shorrosh et al (1992) Chlorophyll b deficiency CAO (Os10g0567400) Morita et al (2005) substitution in pla1-g2 (GAG → GTG) resulted in an amino acid substitution of 407th glutamic acid to valine. The other two short plastochron mutants had DNA lesions in PLA2.…”

Section: Waxy Mutantsmentioning

confidence: 99%

Molecular characterization of mutations induced by gamma irradiation in rice

et al. 2009

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In order to analyze mutations induced by gamma irradiation in higher plants, we irradiated rice with gamma rays and screened for mutations expressing phenotypes of glutinous endosperm (wx), chlorophyll b deficiency, endosperm protein deficiency, gibberellin-related dwarfism, and shortened plastochron-in order to clarify types of mutations. Nucleotide sequence analysis showed that the most frequent mutation induced by gamma rays was deletion, particularly small deletion. Of the 24 mutations, 15 were small deletions (1-16 bp), four were large deletions (9.4 -129.7 kbp), three were single-base substitutions, and two were inversions. Deletions 100 bp-8 kbp in length were not found, suggesting that gamma irradiation is unlikely to induce deletions of 100 bp to 8 kbp but is more likely to induce deletions between 1 and several ten bp or those of around 10 kbp or more. Based on the results, reverse genetics applications may be possible for gamma irradiation-induced deletions in rice by mismatch cleavage analysis used in Targeting Induced Local Lesions IN Genomes (TILLING) to detect small deletions and base substitutions or by using array comparative genomic hybridization (aCGH) to detect large deletions.

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The structure of rice storage protein glutelin precursor deduced from cDNA

Cited by 59 publications

References 12 publications

Molecular Characterization of Oat Seed Globulins

Molecular Characterization of Oat Seed Globulins

Heterogeneity in Subunit Composition of Glutelin in Rice Protein Bodies

Molecular characterization of mutations induced by gamma irradiation in rice

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