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Journal of Integrative Agriculture  2014, Vol. 13 Issue (2): 290-298    DOI: 10.1016/S2095-3119(13)60358-5
Crop Genetics · Breeding · Germplasm Resources Advanced Online Publication | Current Issue | Archive | Adv Search |
Identification of a Group of Novel γ-Gliadin Genes
 QI Peng-fei, WEI Yu-ming, Ouellet Thérèse, CHEN Qing, WANG Zhao, WEI Zhen-zhen , ZHENG You-liang
1.Triticeae Research Institute, Sichuan Agricultural University, Chengdu 611130, P.R.China
2.Agriculture & Agri-Food Canada, Eastern Cereal and Oilseed Research Centre, Ottawa K1A 0C6, Canada
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摘要  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.

Abstract  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.
Keywords:  γ-gliadin       cysteine       disulphide bond       illegitimate recombination  
Received: 07 January 2013   Accepted:
Fund: 

This research was finically supported by the National Natural Science Foundation of China (31230053).

Corresponding Authors:  ZHENG You-liang, Tel: +86-835-2882007, Fax: +86-835-2882153, E-mail: ylzheng@sicau.edu.cn     E-mail:  ylzheng@sicau.edu.cn
About author:  QI Peng-fei, E-mail: pengfeiqi@hotmail.com

Cite this article: 

QI Peng-fei, WEI Yu-ming, Ouellet Thérèse, CHEN Qing, WANG Zhao, WEI Zhen-zhen , ZHENG You-liang. 2014. Identification of a Group of Novel γ-Gliadin Genes. Journal of Integrative Agriculture, 13(2): 290-298.

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