<i>In Vitro</i> Synthesis of Wheat (<i>Triticum aestivum</i> L.) Storage Proteins

Greene, Frank C.

doi:10.1104/pp.68.3.778

Cited by 37 publications

(27 citation statements)

References 17 publications

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“…Preliminary experiments on the immunoprecipitation of in vitro translation products with antibodies raised against avenin have shown the presence of polypeptides migrating near the authentic avenin, some with slightly higher mol wt (not shown), again suggesting synthesis as a precursor containing a signal sequence which is common to other cereal prolamins (5,6,8,12,16 In legumes, a precursor to llS legumin near 60,000 D is synthesized which is later cleaved between disulfide-linked acidic and basic polypeptides (7,22,24). In this respect, the oat globulin is similar.…”

Section: Resultsmentioning

confidence: 99%

Synthesis of Oat Globulin Precursors

Brinegar

Peterson²

1982

Plant Physiol.

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The oat (Avena sativa L.) seed globulin was found to be synthesized in vitro as 60,000 to 64,000 dalton precursors. In vivo protein labeling yielded polypeptides of 58,000 to 62,000 daltons, suggesting cleavage of signal sequences from the precursors. Further cleavage is apparently required to separate the a and ,t polypeptide sequences which are known to form disulfide-linked 53,000 to 58,000 dalton species in the (af)6 holoprotein.The data are discussed with respect to analogous synthesis and processing of some legume 11S storage proteins.The major storage protein of oat seeds is a globulin which comprises as much as 75% of the total seed protein, whereas only 10% is accounted for by the alcohol-soluble prolamin avenin (18). Such a distribution is unusual among cereals, in which the prolamin fraction generally predominates (10). In a recent study, we showed the globulin consisted of heterogeneous sets of a and f8 polypeptides of 32,500 to 37,500 and 22,000 to 24,000 D, and isoelectric points of 5.9 to 7.2 and 8.7 to 9.2, respectively (3). Electrophoretic analysis demonstrated that the a and ,B polypeptides were disulfide-linked in vivo, forming a,8 species of mol wt 53,000 to 58,000 daltons. Based on the holoprotein stoichiometry of six each of the a and ,B polypeptides proposed by Peterson (17), we suggested a native globulin structure of (a,8)6 with an average

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Section: Resultsmentioning

confidence: 99%

Synthesis of Oat Globulin Precursors

Brinegar

Peterson²

1982

Plant Physiol.

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“…Scarcely any [14C~leucine was incorporated into the protein of incubated isolated endosperms (5)(6)(7)(8)(9)(10). But, when isolated endosperms were incubated in a cocktail for cell-free protein synthesis ("Materials and Methods") a high incorporation of [14C] leucine into protein was observed, about 20% ofadded ['4Clleucine being incorporated into TCA-insoluble material within 30 min.…”

Section: And B)mentioning

confidence: 99%

“…Several storage protein polypeptides of cereals (4,8,16,20) and legumes (9,11,24,28) are synthesized as short-lived precursor polypeptides which may undergo modification during or after translation. Some of these precursors seem to be the equivalents of precursor polypeptides of secretory or membrane proteins in that a 'signal' peptide may be present on the polypeptide (2).…”

mentioning

confidence: 99%

Biosynthesis of Storage Proteins in Developing Rice Seeds

Yamagata

Sugimoto²,

Tanaka³

et al. 1982

Plant Physiol.

286

203

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Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis of the starchy endosperm protein of rice (Oryza sativa L. Japonica cv Koshihikari) during seed development confirmed that storage protein begins to accumulate about 5 days after flowering. Two polypeptide groups, 22 to 23 and 37 to 39 kilodaltons, the components of glutelin, the major storage protein in rice seed, appeared 5 days after flowering. A 26-kilodalton polypeptide, the globulin component, also appeared 5 days after flowering. Smaller polypeptides (10-to 16-kilodaltons) including prolamin components, appeared about 10 days after flowering. In contrast, the levels of the 76-and 57-kilodalton polypeptides were fairly constant throughout seed development. Transmission electron microscopy and fractionation by sucrose density gradient centrifugation of the starchy endosperms at various stages of development showed that protein body type II, the accumulation site of glutelin and globulin, was formed faster than protein body type I, the accumulation site of prolamin.The 57-kilodalton polypeptide but not the glutelin subunits was labeled in a 2-hour treatment with I14CIleucine given between 4 and 12 days after flowering to developing ears. In vivo pulse-chase labeling studies showed the 57-kllodalton polypeptide to be a precursor of the 22 to 23 and 37 to 39 kilodalton subunits. The 57-kilodalton polypeptide was salt-soluble, but the mature glutelin subunits were almost salt insoluble.In vitro protein synthesis also showed that the mRNAs directly coding the 22 to 23 and 37 to 39 kilodalton components were absent in developing seeds and that the 57-kilodalton polypeptide was the major product. Thus, it was concluded that the two subunits of rice glutelin are formed through post-translational cleavage of the 57-kilodalton polypeptide.The major storage proteins of most cereal grains are glutelin and prolamin. In rice grains, however, glutelin is the major protein of the starchy endosperm, constituting at least 80%o of the total protein, prolamin accounting for less than 5% (12). Rice glutelin has a mol wt of 6 x I05 according to Tecson et al. (27), but Takeda et a!. (25) demonstrated that it has a heterogeneous mol wt. The increase in glutelin in the developing rice grain coincides with the appearance of PB' in the starchy endosperm 7 to 8 DAF (7,29), and glutelin is found exclusively in PB (7,26,30). In a previous paper (26), we reported two types of PB in the starchy endosperm of rice grains and described their isolation. One (type I, PB-I) is spherical with a concentric ring structure, whereas the other (type II, PB-II) is stained homogeneously by osmium tetroxide and does not have this structure. PB-I contains prolamin, and PB-II is rich in glutelin and globulin. The glutelin in PB-II is composed of two principal subunits, the 22-to 23-and 37-to 39-kD complexes, and the prolamin in PB-I is composed mainly of 13-kD polypeptide.

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“…The prolamin system differs in several aspects According to the available data, many legume from the globulin system detailed above. Direct globulins and cereal prolamins possess N-terminal evidence for the distinct mode of the intracellular signal peptides [17, 22,26,51]. This is to be expected deposition of a cereal prolamin, maize zein, from since both globulins and prolamins are synthesized that of the legume globulins was provided by the on membrane-bound polysomes [52].…”

Section: Discriminatory Factors In Globulin and Prolamin Topogenesismentioning

confidence: 99%

Compartmentalization of seed reserve proteins

Adeli

Altosaar

1984

FEBS Letters

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Two types of storage pathways are proposed for the synthesis and compartmentalization of seed reserve globulins and prolamins. A discussion of the regulatory mechanisms in reserve protein topogenesis reveals that certain factors such as solubility characteristics of the protein molecule and/or specific sorting sequences may underline the discrimination in deposition of globulins and prolamins. Finally, a hypothetical relationship between the type of storage pathway and the seed protein concentration is briefly discussed.

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In Vitro Synthesis of Wheat (Triticum aestivum L.) Storage Proteins

Cited by 37 publications

References 17 publications

Synthesis of Oat Globulin Precursors

Synthesis of Oat Globulin Precursors

Biosynthesis of Storage Proteins in Developing Rice Seeds

Compartmentalization of seed reserve proteins

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