Yan Wanga, 1, Qing-Yun Zhenga, 1, Zhen-Ru Guoa, Yuan-Yuan Qiaoa, Yong-Li Caoa, Cai-Hong Liub, Bin-Jie Xua, Zheng-Yuan Weia, Lu-Juan Zonga, Chen Chena, Ya-Nan Hana, Qing Chena, Xi Gongb, Shi-Yu Huab, You-Liang Zhenga, *, Peng-Fei Qia,*, Yu-Ming Weia, Xiu-Jin Lana, Ji-Rui Wanga
a Triticeae Research Institute, Sichuan Agricultural University, Chengdu, Sichuan 611130, China
b Agronomy College, Sichuan Agricultural University, Chengdu, Sichuan 611130, China
* Corresponding authors.
1 Contributed equally to this paper.
http://dx.doi.org/10.1016/j.aggene.2016.09.001
Highlights
•A Dy10 mutant subunit (Dy10-m328SF) moved faster than Dy10 in SDS-PAGE.
•The faster mobility of Dy10-m328SF was due to a missense mutation in the repetitive domain.
Abstract
High-molecular-weight glutenin subunits (HMW-GS) are important in wheat end-use quality. We characterized a HMW-GS Dy10 mutant subunit with faster mobility than Dy10 in SDS-PAGE, and with equal mobility to Dy10 in urea-containing SDS-PAGE gel. A missense mutation was identified in the mutant subunit, which led to substitution of the 328th amino acid residue from ser (S) to phe (F) in the repetitive domain. The Dy10 subunit containing the missense mutation was designated as Dy10-m328SF (Genbank No. KU934284). Our results indicate that a single amino acid substitution in the repetitive domain can change the mobility of Dy10.
Keywords
HMW-GS; Mutant; Urea; Wheat
Location：