Identiifcation of a Group of Novel γ-Gliadin Genes

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γ-Gliadins are an important component of wheat seed storage proteins. Four novel γ-gliadin genes (Gli-ng1 toGli-ng4) were cloned from wheat (Triticum aestivum) andAegilops species. The novel γ-gliadins were much smaller in molecular size when compared to the typical γ-gliadins, which was caused by deletion of the non-repetitive domain, glutamine-rich region, 3′ part of the repetitive domain, and 5′ part of the C-terminal, possibly due to illegitimate recombination between the repetitive domain and the C-terminal. As a result,Gli-ng1 andGli-ng4 only contained two and three cysteine residues, respectively. Gli-ng1, as the representative of novel γ-gliadin genes, has been sub-cloned into anEscherichia coli expression system. SDS-PAGE indicated that the both cysteine residues ofGli-ng1 could participate in the formation of intermolecular disulphide bondsin vitro. Successful cloning ofGli-ng1 from seed cDNA ofT. aestivumcv. Chinese Spring suggested that these novel γ-gliadin genes were normally transcribed during the development of seeds. Phylogenic analysis indicated that the four novel γ-gliadin genes had a closer relationship with those from the B (S) genome of wheat.
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