Effect of extra cysteine residue of new mutant 1Ax1 subunit on the functional properties of common wheat

Abstract Subunit pair 1Dx5 + 1Dy10 was recognized as superior subunit combination in wheat and contained an extra repetitive-domain cysteine residue in 1Dx5 that was important for understanding the formation of dough viscoelasticity. In this research, one specific serine codon of the 1Ax1 gene corre...

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Autores principales:	Miao Li, Yaqiong Wang, Fengyun Ma, Jian Zeng, Junli Chang, Mingjie Chen, Kexiu Li, Guangxiao Yang, Yuesheng Wang, Guangyuan He
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/bceaf98f309c4dd79a45c034385eadb1
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spelling	oai:doaj.org-article:bceaf98f309c4dd79a45c034385eadb12021-12-02T16:08:19ZEffect of extra cysteine residue of new mutant 1Ax1 subunit on the functional properties of common wheat10.1038/s41598-017-07541-w2045-2322https://doaj.org/article/bceaf98f309c4dd79a45c034385eadb12017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-07541-whttps://doaj.org/toc/2045-2322Abstract Subunit pair 1Dx5 + 1Dy10 was recognized as superior subunit combination in wheat and contained an extra repetitive-domain cysteine residue in 1Dx5 that was important for understanding the formation of dough viscoelasticity. In this research, one specific serine codon of the 1Ax1 gene corresponding to the extra cysteine residue of 1Dx5 was substituted by a cysteine codon through site-directed mutagenesis. Four homozygous transgenic lines (T4) expressing the mutant 1Ax1 gene (mut1Ax1) were produced. Their greater dough strength and stability were confirmed by mixograph and were associated with highly increased gluten index, larger amounts of gluten macropolymers, larger size distribution for glutenin macropolymer particles and varied sodium-dodecyl-sulfate sedimentation volumes, compared with those of the one line expressing wild 1Ax1 that had similar expression level of transgene. The contents of β-sheets in dough and disulfide groups in gluten of the mut1Ax1 transgenic lines were significantly increased. The microstructure of dough mixed to peak showed a more continuous gluten matrix in the mutant transgenic lines than the one line mentioned-above. It was concluded that the extra cysteine residue of mutant 1Ax1 subunit plays a positive role in contributing to dough strength and stability of wheat by cross-linking into gluten aggregates through inter-chain disulfide bonds.Miao LiYaqiong WangFengyun MaJian ZengJunli ChangMingjie ChenKexiu LiGuangxiao YangYuesheng WangGuangyuan HeNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Miao Li Yaqiong Wang Fengyun Ma Jian Zeng Junli Chang Mingjie Chen Kexiu Li Guangxiao Yang Yuesheng Wang Guangyuan He Effect of extra cysteine residue of new mutant 1Ax1 subunit on the functional properties of common wheat
description	Abstract Subunit pair 1Dx5 + 1Dy10 was recognized as superior subunit combination in wheat and contained an extra repetitive-domain cysteine residue in 1Dx5 that was important for understanding the formation of dough viscoelasticity. In this research, one specific serine codon of the 1Ax1 gene corresponding to the extra cysteine residue of 1Dx5 was substituted by a cysteine codon through site-directed mutagenesis. Four homozygous transgenic lines (T4) expressing the mutant 1Ax1 gene (mut1Ax1) were produced. Their greater dough strength and stability were confirmed by mixograph and were associated with highly increased gluten index, larger amounts of gluten macropolymers, larger size distribution for glutenin macropolymer particles and varied sodium-dodecyl-sulfate sedimentation volumes, compared with those of the one line expressing wild 1Ax1 that had similar expression level of transgene. The contents of β-sheets in dough and disulfide groups in gluten of the mut1Ax1 transgenic lines were significantly increased. The microstructure of dough mixed to peak showed a more continuous gluten matrix in the mutant transgenic lines than the one line mentioned-above. It was concluded that the extra cysteine residue of mutant 1Ax1 subunit plays a positive role in contributing to dough strength and stability of wheat by cross-linking into gluten aggregates through inter-chain disulfide bonds.
format	article
author	Miao Li Yaqiong Wang Fengyun Ma Jian Zeng Junli Chang Mingjie Chen Kexiu Li Guangxiao Yang Yuesheng Wang Guangyuan He
author_facet	Miao Li Yaqiong Wang Fengyun Ma Jian Zeng Junli Chang Mingjie Chen Kexiu Li Guangxiao Yang Yuesheng Wang Guangyuan He
author_sort	Miao Li
title	Effect of extra cysteine residue of new mutant 1Ax1 subunit on the functional properties of common wheat
title_short	Effect of extra cysteine residue of new mutant 1Ax1 subunit on the functional properties of common wheat
title_full	Effect of extra cysteine residue of new mutant 1Ax1 subunit on the functional properties of common wheat
title_fullStr	Effect of extra cysteine residue of new mutant 1Ax1 subunit on the functional properties of common wheat
title_full_unstemmed	Effect of extra cysteine residue of new mutant 1Ax1 subunit on the functional properties of common wheat
title_sort	effect of extra cysteine residue of new mutant 1ax1 subunit on the functional properties of common wheat
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/bceaf98f309c4dd79a45c034385eadb1
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Effect of extra cysteine residue of new mutant 1Ax1 subunit on the functional properties of common wheat

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