Comparison of the protein compositions of selected corns and their wild relatives, teosinte and Tripsacum

Paulis, J.W.; Wall, Joseph S.

doi:10.1021/jf60210a022

Cited by 48 publications

(48 citation statements)

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“…1). Our results are consistent with those of Paulis and Wall (1977), where they found protein levels of 28.7% in their parviglumis teosinte accession. The protein content of teosinte was almost as high as protein levels obtained by the Illinois Long-Term Selection Experiment (Dudley 2007) without a corresponding change in the embryo to endosperm ratio (Bjarnason and Pollmer 1972).…”

Section: Kernel Composition and Seed Characteristicssupporting

confidence: 92%

“…The essential amino acids lysine, tryptophan, and methionine are limited because they are lacking or present at low levels in zeins, the major class of storage proteins. Zeins constitute about half of the endosperm protein, and thus nearly half of the total seed protein (Paulis and Wall 1977). Genetic and genomic studies have revealed great complexity of zein gene families (Song et al 2001;Song and Messing 2002;Wilson and Larkins 1984;Woo et al 2001) and support earlier observations that diVerent classes of zeins have varying amino acid compositions (Melcher and Fraij 1980;Sodek and Wilson 1971).…”

Section: Introductionsupporting

confidence: 57%

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Wide variability in kernel composition, seed characteristics, and zein profiles among diverse maize inbreds, landraces, and teosinte

2009

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All crop species have been domesticated from their wild relatives, and geneticists are just now beginning to understand the consequences of artificial (human) selection on agronomic traits that are relevant today. The primary consequence is a basal loss of diversity across the genome, and an additional reduction in diversity for genes underlying traits targeted by selection. An understanding of attributes of the wild relatives may provide insight into target traits and valuable allelic variants for modern agriculture. This is especially true for maize (Zea mays ssp. mays), where its wild ancestor, teosinte (Z. mays ssp. parviglumis), is so strikingly different than modern maize. One obvious target of selection is the size and composition of the kernel. We evaluated kernel characteristics, kernel composition, and zein profiles for a diverse set of modern inbred lines, teosinte accessions, and landraces, the intermediate between inbreds and teosinte. We found that teosinte has very small seeds, but twice the protein content of landraces and inbred lines. Teosinte has a higher average alpha zein content (nearly 89% of total zeins as compared to 72% for inbred lines and 76% for landraces), and there are many novel alcohol-soluble proteins in teosinte relative to the other two germplasm groups. Nearly every zein protein varied in abundance among the germplasm groups, especially the methionine-rich delta zein protein, and the gamma zeins. Teosinte and landraces harbor phenotypic variation that will facilitate genetic dissection of kernel traits and grain quality, ultimately leading to improvement via traditional plant breeding and/or genetic engineering. Abstract All crop species have been domesticated from their wild relatives, and geneticists are just now beginning to understand the consequences of artiWcial (human) selection on agronomic traits that are relevant today. The primary consequence is a basal loss of diversity across the genome, and an additional reduction in diversity for genes underlying traits targeted by selection. An understanding of attributes of the wild relatives may provide insight into target traits and valuable allelic variants for modern agriculture. This is especially true for maize (Zea mays ssp. mays), where its wild ancestor, teosinte (Z. mays ssp. parviglumis), is so strikingly diVerent than modern maize. One obvious target of selection is the size and composition of the kernel. We evaluated kernel characteristics, kernel composition, and zein proWles for a diverse set of modern inbred lines, teosinte accessions, and landraces, the intermediate between inbreds and teosinte. We found that teosinte has very small seeds, but twice the protein content of landraces and inbred lines. Teosinte has a higher average alpha zein content (nearly 89% of total zeins as compared to 72% for inbred lines and 76% for landraces), and there are many novel alcohol-soluble proteins in teosinte relative to the other two germplasm groups. Nearly every zein protein varied in abundance among the germplasm...

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Section: Kernel Composition and Seed Characteristicssupporting

confidence: 92%

Section: Introductionsupporting

confidence: 57%

Wide variability in kernel composition, seed characteristics, and zein profiles among diverse maize inbreds, landraces, and teosinte

2009

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“…This hypothesis has been confirmed by electrophoresis in urea gels (19,21), gel filtration in the presence of urea (19), and SDS-PAGE2 (18,20). The zein II fraction contains all of the polypeptides of the zein I fraction, but in addition contains two or more polypeptides of greater cathodal mobility at pH 2.9 (21) and lower mol wt (18,20) than the zein I fraction polypeptides. Amino acid analyses of the low mol wt fractions from gel filtration confirmed the high methionine content of the smaller polypeptides (19).…”

mentioning

confidence: 88%

“…Zein II contains onefourth to one-half the amount of protein in zein I (7,21 I protein with 10 to 20o of a protein fraction rich in methionine and glycine and deficient in leucine, isoleucine, phenylalanine and aspartic acid and/or its amide (7,21). This hypothesis has been confirmed by electrophoresis in urea gels (19,21), gel filtration in the presence of urea (19), and SDS-PAGE2 (18,20). The zein II fraction contains all of the polypeptides of the zein I fraction, but in addition contains two or more polypeptides of greater cathodal mobility at pH 2.9 (21) and lower mol wt (18,20) than the zein I fraction polypeptides.…”

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confidence: 89%

In Vitro Synthesis of a Precursor to the Methionine-rich Polypeptide of the Zein Fraction of Corn

Melcher¹

1979

Plant Physiol.

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The messenger ribonucleic acid fraction isolated from a protein bodyenriched fraction of developing corn (Zea mays L.) endosperm stimulated the incorporation of radioactive amino acids into at least five polypeptides when added to a wheat germ extract capable of protein synthesis. Of these, the two major polypeptides formed with messenger from freshly frozen corn were identified as precursors to zein A and B, the two major polypeptides of the prolamine fraction of corn meal (21,600 and 19,600 molecular weight). The identification was based on the relative incorporations of radioactive leucine, lysine, and methionine, and the susceptibility of the zein A precursor, but not the zein B precursor to cleavage wtih cyanogen bromide. Using extracts from stored frozen corn, a third polypeptide of 14,500 molecular weight was identified as a major in vitro product. It was preferentially labeled with methionine and slightly larger than a similar peptide in the zein fraction of corn meal. Two other polypeptides of still lower molecular weight could be detected above the background of probably incomplete polypeptides.A major portion of the storage protein of corn endosperm is synthesized on ribosomes bound to ER and protein body membranes (4). Protein bodies are accretions of insoluble protein surrounded by a membrane on which ribosomes are bound. The bodies arise by pinching off from the ER (6). The polypeptide products of translation of these ribosomes must pass through the membrane and accumulate in the interior of the protein body. In other cases where a newly synthesized polypeptide is transported through a membrane, the initial product of translation has an Nterminal extension rich in hydrophobic amino acids, which it is postulated serves as a signal for transmembrane movement of the polypeptide (2). The bound ribosomes of corn have provided the starting material for the isolation of mRNA specific for the synthesis of corn storage proteins (5,9).The protein inside the protein bodies is of the zein or alcoholsoluble fraction of corn proteins. Two polypeptides, zein A and zein B (21,600 and 19,600 mol wt, respectively) make up the bulk of this protein fraction. These correspond to Z1 and Z2 of Lee et al. (11). Several other polypeptides of lower mol wt are also present in zein extracts (11). Extraction of corn meal with an alcoholic solvent followed by an alcoholic solvent containing a reducing agent has led to the isolation of two corn prolamine fracti'ons, designated zein I and zein II. Zein II contains onefourth to one-half the amount of protein in zein I (7,21 I protein with 10 to 20o of a protein fraction rich in methionine and glycine and deficient in leucine, isoleucine, phenylalanine and aspartic acid and/or its amide (7,21). This hypothesis has been confirmed by electrophoresis in urea gels (19,21), gel filtration in the presence of urea (19), and 20). The zein II fraction contains all of the polypeptides of the zein I fraction, but in addition contains two or more polypeptides of greater cathodal mobi...

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“…The presumed ancestral forms and evolutionary patterns of chickpea [49], maize [50], wheat [51] and soybean [52,53] have been identified and established by studying the electrophoretic variability of their respective seed proteins. Gepts [54] used phaseolin as an evolutionary marker in his insightful review of the domestication pattern and world-wide dispersal of the French bean.…”

Section: Phaseolin Polypeptides As Evolutionary Markers -French Bean mentioning

confidence: 99%

Phaseolin: Structure and Evolution

Emani¹,

Hall²

2008

TOEVOLJ

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Abstract:Phaseolin is the salt-soluble glycoprotein or the group of polypeptides of the French bean (Phaseolus vulgaris L.) that account for some 50% of the total protein in mature bean seeds. It was one of the first plant proteins to be translated in vitro from mRNA and one of the first plant genes isolated. It was also the first developmentally regulated plant gene to be expressed in a heterologous plant species through Agrobacterium-mediated transformation. Studies on phaseolin have provided insight to many aspects of plant protein synthesis, from fundamental molecular mechanisms to practical goals such as the improvement of the French bean's nutritional quality. The present review is a comprehensive account of the structural and functional features of phaseolin that have implications regarding its evolution. Additionally, future directions in phaseolin evolutionary studies and suggestions regarding effective and safe biotechnological approaches for the nutritional improvement of French bean seed are outlined.

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Comparison of the protein compositions of selected corns and their wild relatives, teosinte and Tripsacum

Cited by 48 publications

References 10 publications

Wide variability in kernel composition, seed characteristics, and zein profiles among diverse maize inbreds, landraces, and teosinte

Wide variability in kernel composition, seed characteristics, and zein profiles among diverse maize inbreds, landraces, and teosinte

In Vitro Synthesis of a Precursor to the Methionine-rich Polypeptide of the Zein Fraction of Corn

Phaseolin: Structure and Evolution

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