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Analysis of novel high-molecular-weight prolamins from Leymus multicaulis (Kar. et Kir.) Tzvelev and L. chinensis (Trin. ex Bunge) Tzvelev

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Abstract

Nine novel high-molecular-weight prolamins (HMW-prolamins) were isolated from Leymus multicaulis and L. chinensis. Based on the structure of the repetitive domains, all nine genes were classified as D-hordeins but not high-molecular-weight glutenin subunits (HMW-GSs) that have been previously isolated in Leymus spp. Four genes, Lmul 1.2, 2.4, 2.7, and Lchi 2.5 were verified by bacterial expression, whereas the other five sequences (1.3 types) were classified as pseudogenes. The four Leymus D-hordein proteins had longer N-termini than those of Hordeum spp. [116/118 vs. 110 amino acid (AA) residues], whereas three (Lmul 1.2, 2.4, and 2.7) contained shorter N-termini than those of the Ps. juncea (116 vs. 118 AA residues). Furthermore, Lmul 1.2 was identified as the smallest D-hordein, and Lmul 1.2 and 2.7 had an additional cysteines. Phylogenetic analysis supported that the nine D-hordeins of Leymus formed two independent clades, with all the 1.3 types clustered with Ps. juncea Ns 1.3, whereas the others were clustered together with the D-hordeins from Hordeum and Ps. juncea and the HMW-GSs from Leymus. Within the clade of four D-hordein genes and HMW-GSs, the HMW-GSs of Leymus formed a separated branch that served as an intermediate between the D-hordeins of Ps. juncea and Leymus. These novel D-hordeins may be potentially utilized in the improvement of food processing properties particularly those relating to extra cysteine residues. The findings of the present study also provide basic information for understanding the HMW-prolamins among Triticeae species, as well as expand the sources of D-hordeins from Hordeum to Leymus.

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Abbreviations

AA:

Amino acid

CS:

Chinese spring

HMW-GSs:

High molecular weight glutenin subunits

HMW-prolamins:

High-molecular-weight prolamins

ORFs:

Open reading frames

SDS-PAGE:

Sodium dodecyl sulfate polyacrylamide gel electrophoresis

Sh:

Shinchunaga

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Acknowledgements

The Ministry of Science and Technology of China (2016YFD0100502, 2017YFD0100903), the National Natural Science Foundation of China (U1403185, 31771783), and the Key Fund Project of the Sichuan Provincial Department of Education (15ZA0021) supported this study. Hu XK was supported by the China Scholarship Council under the MOE-AAFC PhD Research Program.

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Authors and Affiliations

  1. Triticeae Research Institute, Sichuan Agricultural University, Wenjiang, Chengdu, 611130, Sichuan, People’s Republic of China

    Xinkun Hu, Shoufen Dai, Zhongping Song, Dongyang Xu, Zhaojin Wen, Yuming Wei, Dengcai Liu, Youliang Zheng & Zehong Yan

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  1. Xinkun Hu
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  2. Shoufen Dai
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Correspondence to Zehong Yan.

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Hu, X., Dai, S., Song, Z. et al. Analysis of novel high-molecular-weight prolamins from Leymus multicaulis (Kar. et Kir.) Tzvelev and L. chinensis (Trin. ex Bunge) Tzvelev. Genetica 146, 255–264 (2018). https://doi.org/10.1007/s10709-018-0025-z

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