| Literature DB >> 26940567 |
Zhuo Huang1, Hai Long2, Yu-Ming Wei3, Ze-Hong Yan3, You-Liang Zheng4.
Abstract
The α-gliadins account for 15-30 % of the total storage protein in wheat endosperm and play important roles in the dough extensibility and nutritional quality. On the other side, they act as a main source of toxic peptides triggering celiac disease. In this study, 37 α-gliadins were isolated from three species of Aegilops section Sitopsis. Sequence similarity and phylogenetic analyses revealed novel allelic variation at Gli-2 loci of species of Sitopsis and regular organization of motifs in their repetitive domain. Based on the comprehensive analyses of a large number of known sequences of bread wheat and its diploid genome progenitors, the distributions of four T cell epitopes and length variations of two polyglutamine domains are analyzed. Additionally, according to the organization of repeat motifs, we classified the α-gliadins of Triticum and Aegilops into eight types. Their most recent common ancestor and putative divergence patterns were further considered. This study provides new insights into the allelic variations of α-gliadins in Aegilops section Sitopsis, as well as evolution of α-gliadin multigene family among Triticum and Aegilops species.Entities:
Keywords: Celiac disease; Endosperm storage protein; Gene family; Processing quality; Wheat
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Year: 2016 PMID: 26940567 DOI: 10.1007/s10709-016-9891-4
Source DB: PubMed Journal: Genetica ISSN: 0016-6707 Impact factor: 1.082