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小麦种子蛋白的遗传变异与改良。

Genetic variability and improvement of seed proteins in wheat.

机构信息

Department of Plant Sciences, University of California Riverside, 92502, Ca., USA.

出版信息

Theor Appl Genet. 1977 Mar;51(2):71-9. doi: 10.1007/BF00299480.

DOI:10.1007/BF00299480
PMID:24317598
Abstract

Albumins, globulins, gliadins and glutenins presumably comprising 100 percent of the wheat seed proteins were sequentially extracted and electrophoresed on SDS-polyacrylamide gels. The SDS-electrophoretic patterns within each of the four fractions from T. boeotiaum, T. urartu, T. turgidum, T. timopheevii, T. aestivum, Ae. speltoides and Ae. squawosa were similar. They differed from one species to another only in a few minor components or density of certain components. Similarity in MW's of components, as indicated by the SDS-electrophoretic patterns, suggests that the wheats and Aegilops exhibit no variability for structural genes coding seed proteins. A minimum of 60 to 70 and a maximum of 360 to 420 structural genes with major or minor effects control the total seed protein in T. aestivum. Presumably, only one or the other homoeoallele was expressed in the polyploids. Different components of albumins and globulins presumably had distinct MW's and amino acid composition, while the components of gliadins and glutenins could be classified into a few groups each containing one or more components with the same MW and nearly identical amino acid composition. The genes for components with similar MW's and amino acid composition arose through multiplication of a single original gene and perhaps share the same regulatory mechanism. Seed protein content and quality in wheat might be improved through the incorporation of structural genes, coding for polypeptides with distinct MW's, from distantly related species, rather than by manipulation of the structural genes within the Triticum-Aegilops group. Regulatory mutants similar to opaque-2 of corn could be used to alter the proportion of gliadins in relation to albumins and globulins, to improve amino acid composition of wheat proteins.

摘要

白蛋白、球蛋白、醇溶蛋白和谷蛋白可能构成小麦种子蛋白质的 100%,依次用 SDS-聚丙烯酰胺凝胶进行提取和电泳。T. boeotium、T. urartu、T. turgidum、T. timopheevii、T. aestivum、Ae. speltoides 和 Ae. squawosa 这四个部分的 SDS-电泳图谱在每个部分都是相似的。它们在不同的物种之间只有少数的成分或某些成分的密度有所不同。根据 SDS-电泳图谱,成分的 MW 值相似表明小麦和冰草没有结构基因编码种子蛋白的可变性。T. aestivum 中控制总种子蛋白的结构基因至少有 60 到 70 个,最多有 360 到 420 个,具有主要或次要影响。推测在多倍体中只有一个或另一个同源等位基因被表达。白蛋白和球蛋白的不同成分可能具有不同的 MW 值和氨基酸组成,而醇溶蛋白和谷蛋白的成分可以分为几个组,每个组包含一个或多个具有相同 MW 值和几乎相同氨基酸组成的成分。具有相似 MW 值和氨基酸组成的成分的基因可能是通过单个原始基因的倍增产生的,并且可能具有相同的调控机制。通过整合来自远缘物种的具有不同 MW 值和编码多肽的结构基因,而不是通过操纵小麦-冰草组内的结构基因,可以提高小麦的种子蛋白含量和质量。类似于玉米 opaque-2 的调节突变体可用于改变醇溶蛋白与白蛋白和球蛋白的比例,从而改善小麦蛋白的氨基酸组成。

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本文引用的文献

1
Genetic analysis of grain protein percentage in wheat.小麦籽粒蛋白质含量的遗传分析。
Theor Appl Genet. 1975 Jan;46(2):79-86. doi: 10.1007/BF00281646.
2
Chromosomal control of non-gliadin proteins from the 70% ethanol extract of wheat endosperm.小麦胚乳 70%乙醇提取物中非醇溶蛋白的染色体控制。
Theor Appl Genet. 1975 Jan;45(7):322-6. doi: 10.1007/BF00276687.
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Storage Protein Synthesis in Maize: Isolation of Zein-synthesizing Polyribosomes.玉米贮藏蛋白合成:醇溶蛋白合成多核糖体的分离。
Plant Physiol. 1976 May;57(5):740-5. doi: 10.1104/pp.57.5.740.
4
MUTANT GENE THAT CHANGES PROTEIN COMPOSITION AND INCREASES LYSINE CONTENT OF MAIZE ENDOSPERM.改变玉米胚乳蛋白质组成并增加赖氨酸含量的突变基因。
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The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定分子量的可靠性。
J Biol Chem. 1969 Aug 25;244(16):4406-12.
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The D-genome and the control of wheat gluten synthesis.
Experientia. 1969 Mar 15;25(3):317-9. doi: 10.1007/BF02034419.
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The gross conformation of protein-sodium dodecyl sulfate complexes.蛋白质 - 十二烷基硫酸钠复合物的总体构象。
J Biol Chem. 1970 Oct 10;245(19):5161-5.
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Protein subunits in the potato virus X group. Determination of the molecular weights by polyacrylamide electrophoresis.
Biochim Biophys Acta. 1970 Apr 28;207(1):184-9. doi: 10.1016/0005-2795(70)90150-9.
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Electrofocusing of grain proteins from wheat genotypes.小麦基因型籽粒蛋白质的等电聚焦
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Genetic improvement of plant protein.植物蛋白的基因改良。
J Agric Food Chem. 1974 Jul-Aug;22(4):558-66. doi: 10.1021/jf60194a011.