Identification of a Group of Novel γ-Gliadin Genes

Peng Fei Qi, Yu Ming Wei, Ouellet ThéRèse, Qing Chen, Zhao Wang, Zhen Zhen Wei, You Liang Zheng

Research output: Contribution to journalArticlepeer-review


γ-Gliadins are an important component of wheat seed storage proteins. Four novel γ-gliadin genes (Gli-ng1 to Gli-ng4) were cloned from wheat (Triticum aestivum) and Aegilops 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 and Gli-ng4 only contained two and three cysteine residues, respectively. Gli-ng1, as the representative of novel γ-gliadin genes, has been sub-cloned into an Escherichia coli expression system. SDS-PAGE indicated that the both cysteine residues of Gli-ng1 could participate in the formation of intermolecular disulphide bonds in vitro. Successful cloning of Gli-ng1 from seed cDNA of T. aestivum cv. 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.

Original languageEnglish
Pages (from-to)290-298
Number of pages9
JournalJournal of Integrative Agriculture
Issue number2
StatePublished - Feb 2014
Externally publishedYes


  • γ-gliadin
  • Cysteine
  • Disulphide bond
  • Illegitimate recombination

ASJC Scopus subject areas

  • Food Science
  • Biochemistry
  • Ecology
  • Food Animals
  • Animal Science and Zoology
  • Agronomy and Crop Science
  • Plant Science


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