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...

Full description

Bibliographic Details
Main Authors: Miao Li, Yaqiong Wang, Fengyun Ma, Jian Zeng, Junli Chang, Mingjie Chen, Kexiu Li, Guangxiao Yang, Yuesheng Wang, Guangyuan He
Format: Article
Language:English
Published: Nature Publishing Group 2017-08-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-017-07541-w
id doaj-bceaf98f309c4dd79a45c034385eadb1
record_format Article
collection DOAJ
language English
format Article
sources DOAJ
author Miao Li
Yaqiong Wang
Fengyun Ma
Jian Zeng
Junli Chang
Mingjie Chen
Kexiu Li
Guangxiao Yang
Yuesheng Wang
Guangyuan He
spellingShingle 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
Scientific Reports
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 Publishing Group
series Scientific Reports
issn 2045-2322
publishDate 2017-08-01
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.
url https://doi.org/10.1038/s41598-017-07541-w
work_keys_str_mv AT miaoli effectofextracysteineresidueofnewmutant1ax1subunitonthefunctionalpropertiesofcommonwheat
AT yaqiongwang effectofextracysteineresidueofnewmutant1ax1subunitonthefunctionalpropertiesofcommonwheat
AT fengyunma effectofextracysteineresidueofnewmutant1ax1subunitonthefunctionalpropertiesofcommonwheat
AT jianzeng effectofextracysteineresidueofnewmutant1ax1subunitonthefunctionalpropertiesofcommonwheat
AT junlichang effectofextracysteineresidueofnewmutant1ax1subunitonthefunctionalpropertiesofcommonwheat
AT mingjiechen effectofextracysteineresidueofnewmutant1ax1subunitonthefunctionalpropertiesofcommonwheat
AT kexiuli effectofextracysteineresidueofnewmutant1ax1subunitonthefunctionalpropertiesofcommonwheat
AT guangxiaoyang effectofextracysteineresidueofnewmutant1ax1subunitonthefunctionalpropertiesofcommonwheat
AT yueshengwang effectofextracysteineresidueofnewmutant1ax1subunitonthefunctionalpropertiesofcommonwheat
AT guangyuanhe effectofextracysteineresidueofnewmutant1ax1subunitonthefunctionalpropertiesofcommonwheat
_version_ 1724393766130810880
spelling doaj-bceaf98f309c4dd79a45c034385eadb12020-12-08T02:24:53ZengNature Publishing GroupScientific Reports2045-23222017-08-017111310.1038/s41598-017-07541-wEffect of extra cysteine residue of new mutant 1Ax1 subunit on the functional properties of common wheatMiao Li0Yaqiong Wang1Fengyun Ma2Jian Zeng3Junli Chang4Mingjie Chen5Kexiu Li6Guangxiao Yang7Yuesheng Wang8Guangyuan He9The Genetic Engineering International Cooperation Base of Chinese Ministry of Science and Technology, The Key Laboratory of Molecular Biophysics of Chinese Ministry of Education, College of Life Science and Technology, Huazhong University of Science & TechnologyThe Genetic Engineering International Cooperation Base of Chinese Ministry of Science and Technology, The Key Laboratory of Molecular Biophysics of Chinese Ministry of Education, College of Life Science and Technology, Huazhong University of Science & TechnologyThe Genetic Engineering International Cooperation Base of Chinese Ministry of Science and Technology, The Key Laboratory of Molecular Biophysics of Chinese Ministry of Education, College of Life Science and Technology, Huazhong University of Science & TechnologyThe Genetic Engineering International Cooperation Base of Chinese Ministry of Science and Technology, The Key Laboratory of Molecular Biophysics of Chinese Ministry of Education, College of Life Science and Technology, Huazhong University of Science & TechnologyThe Genetic Engineering International Cooperation Base of Chinese Ministry of Science and Technology, The Key Laboratory of Molecular Biophysics of Chinese Ministry of Education, College of Life Science and Technology, Huazhong University of Science & TechnologyThe Genetic Engineering International Cooperation Base of Chinese Ministry of Science and Technology, The Key Laboratory of Molecular Biophysics of Chinese Ministry of Education, College of Life Science and Technology, Huazhong University of Science & TechnologyThe Genetic Engineering International Cooperation Base of Chinese Ministry of Science and Technology, The Key Laboratory of Molecular Biophysics of Chinese Ministry of Education, College of Life Science and Technology, Huazhong University of Science & TechnologyThe Genetic Engineering International Cooperation Base of Chinese Ministry of Science and Technology, The Key Laboratory of Molecular Biophysics of Chinese Ministry of Education, College of Life Science and Technology, Huazhong University of Science & TechnologyThe Genetic Engineering International Cooperation Base of Chinese Ministry of Science and Technology, The Key Laboratory of Molecular Biophysics of Chinese Ministry of Education, College of Life Science and Technology, Huazhong University of Science & TechnologyThe Genetic Engineering International Cooperation Base of Chinese Ministry of Science and Technology, The Key Laboratory of Molecular Biophysics of Chinese Ministry of Education, College of Life Science and Technology, Huazhong University of Science & TechnologyAbstract 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.https://doi.org/10.1038/s41598-017-07541-w