中文摘要：

Gliadins are the major components of storage proteins in wheat and play an important role in determining the extensibility properties of dough. In the present work, six novel full-length γ-gliadin genes were cloned from the C genome of Aegilops markgrafii using a PCR-based strategy. Analysis of the deduced amino acid sequences showed that the cloned genes had primary structures that were similar, but not identical, to published γ-gliadins from other wheat-related species. The lengths of the open reading frames (ORFs) ranged from 909 to 963 bp, and the repetitive and glutamine-rich domains weremainly responsible for the size of the proteins. An extra cysteine residue was present in the repetitive domain of sequence JX566513. All amino acid sequences of γ-gliadin genes from Ae. markgrafii were searched for the five peptides identified as T cell stimulatory epitopes in celiac disease (CD) patients. Peptide Gliγ-3 was present in sequences JX566513 and JX566514. Peptide Gliγ-5 was present only in JX566513. The other γ-gliadins contained no toxic epitopes. These results provide information to better understand the use of Ae. markgrafii in wheat breeding and the evolutionary relationship of the γ-gliadin genes in Ae. markgrafii and other Triticeae species.