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Characterization of high-molecular-weight glutenin subunits from Eremopyrum bonaepartis and identification of a novel variant with unusual high molecular weight and altered cysteine residues

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Abstract

We characterized two high-molecular-weight glutenin subunit (HMW-GS) variants from Eremopyrum bonaepartis, determined their complete open reading frames, and further expressed them in a bacterial system. The variants have many novel structural features compared with typical subunits encoded by Glu-1 loci: 1Fx3.7 and 1Fy1.5 exhibit hybrid properties of x- and y-type subunits. In addition, unusual molecular mass and altered number and distribution of cysteine residues were unique features of HMW-GSs encoded by Glu-F1 from E. bonaepartis. The mature 1Fx3.7 subunit has a full length of 1,223 amino acid residues, making it the largest subunit found thus far, while 1Fy1.5 is just 496 residues. In addition, the mutated PGQQ repeat motif was found in the repetitive region of 1Fx3.7. Although it has a similar molecular mass to that previously reported for 1Dx2.2, 1Dx2.2* and 1Sshx2.9 subunits, 1Fx3.7 appears to have had a different evolutionary history. The N-terminal and repetitive regions have a total of four additional cysteine residues, giving 1Fx3.7 a total of eight cysteines, while 1Fy1.5 has only six cysteines because the GHCPTSPQQ nonapeptide at the end of the repetitive region is deleted. With its extra cysteine residues and the longest repetitive region, features that are relevant to good wheat quality, the 1Fx3.7 subunit gene could be an excellent candidate for applications in wheat quality improvement.

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Abbreviations

aa:

Amino acid

BAC:

Bacterial artificial chromosome

BLAST:

The basic local alignment search tool

CTAB:

Cetyltrimethylammonium bromide

HMW-GS:

High-molecular-weight glutenin subunit

NCBI:

National Center for Biotechnology Information

NJ:

Neighbor-joining trees

ORF:

Open reading frame

SDS-PAGE:

Sodium dodecyl sulfate polyacrylamide gel electrophoresis

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Acknowledgments

This work was supported by the National Natural Science Foundation of China (31230053 and 31000167).

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Authors and Affiliations

  1. Triticeae Research Institute, Sichuan Agricultural University, Chengdu, 611130, Sichuan, China

    Qian-Tao Jiang, Xiao-Wei Zhang, Jian Ma, Long Wei, Shan Zhao, Quan-Zhi Zhao, Peng-Fei Qi & Yu-Ming Wei

  2. Lethbridge Research Centre, Agriculture and Agri-Food Canada, Lethbridge, T1J 4B1, Canada

    Zhen-Xiang Lu

  3. Key Laboratory of Southwestern Crop Germplasm Utilization, Ministry of Agriculture, Sichuan Agricultural University, Ya’an, 625014, Sichuan, China

    You-Liang Zheng

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  1. Qian-Tao Jiang
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Correspondence to Yu-Ming Wei.

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Jiang, QT., Zhang, XW., Ma, J. et al. Characterization of high-molecular-weight glutenin subunits from Eremopyrum bonaepartis and identification of a novel variant with unusual high molecular weight and altered cysteine residues. Planta 239, 865–875 (2014). https://doi.org/10.1007/s00425-013-2021-y

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