Analysis of HMW glutenin subunits and their coding sequences in two diploid Aegilops species
Analysis of HMW glutenin subunits and their coding sequences in two diploid Aegilops species
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DOI：
10.1007/s00122-002-1175-y
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发表时间：
2003-05-01
影响因子：
5.4
通讯作者：
Wang, D.
中科院分区：
文献类型：
--
作者：
Liu, Z.;Yan, Z.;Wang, D.
在了解六倍体小麦高分子量（HMW）麦谷蛋白亚基的结构、功能和遗传调控方面已经取得了相当大的进展。相比之下，人们对小麦相关物种中这些类型的蛋白质知之甚少。在本文中，我们报告了两种二倍体山羊草物种：伞山羊草 (UU) 和有尾山羊草 (CC) 的 HMW 麦谷蛋白亚基及其编码序列的分析。 SDS-PAGE 分析表明，对于四种 Ae 中的每一种。在 umbellulata 种质中，有两个 HMW 麦谷蛋白亚基（此处指定为 1Ux 和 1Uy），其电泳迁移率分别与 Glu-D1 基因座编码的 x 型和 y 型亚基相当。在我们之前的研究中，涉及多种 Ae。在有尾目中，还检测到两个 HMW 麦谷蛋白亚基（指定为 1Cx 和 1Cy），其电泳迁移率与 Glu-D1 基因座控制的亚基相似。这些结果表明，Ae 的 U 基因组。 umbellulata 和 Ae 的 C 基因组。有尾目编码 HMW 麦谷蛋白亚基，其结构可能与 D 基因组指定的亚基相似。克隆并测序了两个二倍体物种中编码 x 型和 y 型 HMW 麦谷蛋白亚基的完整开放阅读框 (ORF)。对推导的氨基酸序列的分析表明，这两个山羊草物种的 x 型和 y 型 HMW 麦谷蛋白亚基的一级结构与先前发表的 HMW 麦谷蛋白亚基的一级结构相似。去除了信号肽编码序列的修饰 ORF 的细菌表达产生了与从种子中提取的 HMW 麦谷蛋白亚基具有相同电泳迁移率的蛋白质，表明种子成熟后，信号肽从两个物种的 HMW 麦谷蛋白亚基中去除。系统发育分析表明，1Ux 和 1Cx 亚基与 Glu-D1 位点编码的 1Dx 型亚基关系最密切。与1Cy亚基相比，1Uy亚基与1Dy型亚基具有更高水平的同源性。总之，我们的研究表明 Ae 的 Glu-U1 位点。 umbellulata 和 Ae 的 Glu-C1 位点。 caudata 以类似于 Glu-D1 基因座的方式指定 HMW 麦谷蛋白亚基的表达。因此，两个二倍体物种的 HMW 麦谷蛋白亚基可能在改善六倍体小麦品种的加工特性方面具有潜在价值。
Considerable progress has been made in understanding the structure, function and genetic regulation of high-molecular-weight (HMW) glutenin subunits in hexaploid wheat. In contrast, less is known about these types of proteins in wheat related species. In this paper, we report the analysis of HMW glutenin subunits and their coding sequences in two diploid Aegilops species, Aegilops umbellulata (UU) and Aegilops caudata (CC). SDS-PAGE analysis demonstrated that, for each of the four Ae. umbellulata accessions, there were two HMW glutenin subunits (designated here as 1Ux and 1Uy) with electrophoretic mobilities comparable to those of the x- and y-type subunits encoded by the Glu-D1 locus, respectively. In our previous study involving multiple accessions of Ae. caudata, two HMW glutenin subunits (designated as 1Cx and 1Cy) with electrophoretic mobilities similar to those of the subunits controlled by the Glu-D1 locus were also detected. These results indicate that the U genome of Ae. umbellulata and the C genome of Ae. caudata encode HMW glutenin subunits that may be structurally similar to those specified by the D genome. The complete open reading frames (ORFs) coding for x- and y-type HMW glutenin subunits in the two diploid species were cloned and sequenced. Analysis of deduced amino acid sequences revealed that the primary structures of the x- and y-type HMW glutenin subunits of the two Aegilops species were similar to those of previously published HMW glutenin subunits. Bacterial expression of modified ORFs, in which the coding sequence for the signal peptide was removed, gave rise to proteins with electrophoretic mobilities identical to those of HMW glutenin subunits extracted from seeds, indicating that upon seed maturation the signal peptide is removed from the HMW glutenin subunit in the two species. Phylogenetic analysis showed that 1Ux and 1Cx subunits were most closely related to the 1Dx type subunit encoded by the Glu-D1 locus. The 1Uy subunit possessed a higher level of homology to the 1Dy-type subunit compared with the 1Cy subunit. In conclusion, our study suggests that the Glu-U1 locus of Ae. umbellulata and the Glu-C1 locus of Ae. caudata specify the expression of HMW glutenin subunits in a manner similar to the Glu-D1 locus. Consequently, HMW glutenin subunits from the two diploid species may have potential value in improving the processing properties of hexaploid wheat varieties.