Special Issue:
麦类遗传育种合辑Triticeae Crops Genetics · Breeding · Germplasm Resources
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Influence of high-molecular-weight glutenin subunit deletions at the Glu-A1 and Glu-D1 loci on protein body development, protein components and dough properties of wheat (Triticum aestivum L.) |
LIU Da-tong*, ZHANG Xiao*, JIANG Wei, LI Man, WU Xu-jiang, GAO De-rong, BIE Tong-de, LU Cheng-bin |
Key Laboratory of Wheat Biology and Genetic Improvement for Low & Middle Yangtze Valley, Ministry of Agriculture and Rural Affairs/Lixiahe Institute of Agricultural Sciences of Jiangsu, Yangzhou 225007, P.R.China
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摘要
本研究以扬麦18为背景构建的四种不同Glu-A1、Glu-D1位点缺失近等基因系为材料,观察了蛋白体发育的形态学特征、测定了蛋白组分和面团特性指标。结果表明,HMW-GS亚基缺失造成了蛋白体发育进程延迟。花后10天开始,HMW-GS缺失系表现为蛋白体发育延迟、体积增长减缓,随着花后时间增加差异减小;至花后25天(胚乳发育中后期),四种近等基因系蛋白体发育状况已无明显差异。与野生型和Glu-A1位点缺失类型相比,Glu-D1位点缺失和Glu-A1、Glu-D1双缺失类型的高/低分子量谷蛋白比值、谷蛋白大聚合体含量、揉混仪参数以及拉伸仪参数降低,醇溶蛋白/谷蛋白比例升高;Glu-D1位点缺失后面团强度和延展性显著降低。本研究全面分析了HMW-GS缺失影响蛋白体发育、蛋白性状和面团特性的效应,为Glu-D1位点缺失种质在弱筋小麦品质改良中的应用提供了理论支撑,并提供了改良饼干、蛋糕、南方馒头和酿酒等原料弱筋小麦品质的新途径。
Abstract
High-molecular-weight glutenin subunits (HMW-GSs) play a critical role in determining the viscoelastic properties of wheat. As the organelle where proteins are stored, the development of protein bodies (PBs) reflects the status of protein synthesis and also affects grain quality to a great extent. In this study, with special materials of four near-isogenic lines in a Yangmai 18 background we created, the effects of Glu-A1 and Glu-D1 loci deletions on the development and morphological properties of the protein body, protein components and dough properties were investigated. The results showed that the deletion of the HMW-GS subunit delayed the development process of the PBs, and slowed the increases of volume and area of PBs from 10 days after anthesis (DAA) onwards. In contrast, the areas of PBs at 25 DAA, the middle or late stage of endosperm development, showed no distinguishable differences among the four lines. Compared to the wild type and single null type in Glu-A1, the ratios of HMW-GSs to low-molecular-weight glutenin subunits (LMW-GSs), glutenin macropolymer (GMP) content, mixograph parameters as well as extension parameters decreased in the single null type in Glu-D1 and double null type in Glu-A1 and Glu-D1, while the ratios of gliadins (Gli)/glutenins (Glu) in those types increased. The absence of Glu-D1 subunits decreased both dough strength and extensibility significantly compared to the Glu-A1 deletion type. These results provide a detailed description of the effect of HMW-GS deletion on PBs, protein traits and dough properties, and contribute to the utilization of Glu-D1 deletion germplasm in weak gluten wheat improvement for use in cookies, cakes and southern steamed bread in China and liquor processing.
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Received: 20 October 2020
Accepted: 18 December 2020
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Fund: This work was supported by the National Key Research and Development Program of China (2016YFD0100500), the Natural Science Foundation of Jiangsu Province, China (BK20160448) and the National Natural Science Foundation of China (32071999 and 31700163). |
About author: LIU Da-tong, Tel: +86-514-87303868, E-mail: ldt@wheat.org.cn; ZHANG Xiao, Tel: +86-514-87303868, E-mail: zx@wheat.org.cn; Correspondence LU Cheng-bin, Tel: +86-514-87307821, E-mail: lucb123@126.com
* These authors contributed equally to this study. |
Cite this article:
LIU Da-tong, ZHANG Xiao, JIANG Wei, LI Man, WU Xu-jiang, GAO De-rong, BIE Tong-de, LU Cheng-bin.
2022.
Influence of high-molecular-weight glutenin subunit deletions at the Glu-A1 and Glu-D1 loci on protein body development, protein components and dough properties of wheat (Triticum aestivum L.). Journal of Integrative Agriculture, 21(7): 1867-1876.
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Arcalis E, Marcel S, Altmann F, Kolarich D, Drakakaki G, Fischer R, Christou P, Stoger E. 2004. Unexpected deposition patterns of recombinant proteins in post-endoplasmic reticulum compartments of wheat endosperm. Plant Physiology, 136, 3457–3466.
Bangur R, Batey I L, McKenzie E, MacRitchie F. 1997. Dependence of extensograph parameters on wheat protein composition measured by SE-HPLC. Journal of Cereal Science, 25, 237–241.
Beasley H L, Uthayakumaran S, Stoddard F L, Partridge S J, Daqiq L, Chong P, Bekes F. 2002. Synergistic and additive effects of three high molecular weight glutenin subunit loci. II. Effects on wheat dough functionality and end-use quality. Cereal Chemistry, 79, 301–307.
Belitz H D, Grosch W, Schieberle P. 2009. Food Chemistry. Springer Verlag, Germany. pp. 670–710.
Branlard G, Dardevet M. 1985. Diversity of grain protein and bread wheat quality: II. Correlation between high molecular weight subunits of glutenin and flour quality characteristics. Journal of Cereal Science, 3, 345–354.
Chen X Y, Li B, Shao S S, Wang L L, Zhu X W, Yang Y, Wang W J, Yu X R, Xiong F. 2016. Accumulation characteristic of protein bodies in different regions of wheat endosperm under drought stress. Journal of Integrative Agriculture, 15, 2921–2930.
Cho S W, Kang C S, Ko H S, Baik B K, Cho K M, Park C S. 2018. Influence of protein characteristics and the proportion of gluten on end-use quality in Korean wheat cultivars. Journal of Integrative Agriculture, 17, 1706–1719.
Deng Z Y, Tian J C, Sun G X. 2005. Influence of high molecular weight glutenin subunit substitution on rheological behavior and bread-baking quality of near-isogenic lines developed from Chinese wheats. Plant Breeding, 124, 428–431.
Galili G, Altschuler Y, Levanony H. 1993. Assembly and transport of seed storage proteins. Trends in Cell Biolopy, 3, 437–443.
Galili G, Shimoni Y, Giorini-Silfen S, Levanony H, Altschuler Y, Shani N. 1996. Wheat storage proteins: Assembly, transport and deposition in protein bodies. Plant Physiology and Biochemistry, 34, 245–252.
Gil-Humanes J, Pistón F, Giménez M J, Martín A, Francisco B. 2012. The introgression of RNAi silencing of γ-gliadins into commercial lines of bread wheat changes the mixing and technological properties of the dough. PLoS ONE, 7, e45937.
Gupta R B, Batey I L, MacRitchie F.1992. Relationships between protein composition and functional properties of wheat flours. Cereal Chemistry, 69, 125–131.
Gupta R B, MacRitchie F, Shepherd K W, Ellison F W. 1991. Relative contribution of LMW and HMW subunits of glutenin to dough strength and dough stickiness of bread wheat. In: Bushuk W, Tkachuk R, eds., Gluten Proteins 1990. American Association of Cereal Chemists, St. Paul, MN. pp. 71–78.
Halford N G, Field J M, Blair H, Urwin P, Moore K, Robert L, Thompson R, Flavell R B, Tatham A S, Shewry P R. 1992. Analysis of HMW glutenin subunits encoded by chromosome 1A of bread wheat (Triticum aestivum L.) indicates quantitative effects on grain quality. Theoretical & Applied Genetics, 83, 373–378.
Herman E M, Larkins B A. 1999. Protein storage bodies and vacuoles. The Plant Cell, 11, 601–613.
Kim J E, Baik B K, Park C S, Son J H, Choi C H, Mo Y, Park T I, Kang C S, Cho S W. 2019. Relationship between physicochemical characteristics of Korean wheat flour and quality attributes of steamed bread. Journal of Integrative Agriculture, 18, 2652–2663.
Lawrence G J, MacRitchie F, Wrigley C W. 1988. Dough and baking quality of wheat lines deficient in glutenin subunits controlled by the Glu-A1, Glu-B1 and Glu-D1 loci. Journal of Cereal Science, 7, 109–112.
Liu H Y, Wang W Q, Li X, Wang K, Wang L, Du L P, Yan Y M, Ye X G. 2017. Glu-B1 silencing influences protein body formation and expression of genes regulating synthesis and processing of seed-storage protein in somatic mutant wheat AS208. Acta Agronomica Sinica, 43, 691–700. (in Chinese)
Ma W, Apples R, Bekes F, Larroque O, Morell M K, Gale K R. 2005. Genetic characterisation of dough rheological properties in a wheat doubled haploid population: Additive genetic effects and epistatic interactions. Theoretical & Applied Genetics, 111, 410–422.
MacRitchie F. 2014. Theories of glutenin/dough systems. Journal of Cereal Science, 60, 4–6.
Majoul T, Bancel E, Triboi E, Ben H J, Branlard G. 2004. Proteomic analysis of the effect of heat stress on hexaploid wheat grain: Charaterization of heat-responsive proteins from non-prolamins fraction. Proteomics, 4, 505–513.
Metakovsky E V, Novoselskaya A Y, Sozinov A A. 1984. Genetic analysis of gliadin components in winter wheat using two-dimensional polyacrylamide gel electrophoresis. Theoretical & Applied Genetics, 69, 31–37.
Mondal S, Tilley M, Alviola J N, Waniska R D, Bean S R, Glover K D, Hays D B. 2008. Use of near-isogenic wheat lines to determine the glutenin composition and functionality requirements for flour tortillas. Journal of Agricultural & Food Chemistry, 56, 179–184.
Müntz K. 1998. Deposition of storage proteins. Plant Molecular Biology, 38, 77–99.
Payne P I, Lawrence G J. 1983. Catalogue of alleles for the complex gene loci, Glu-A1, Glu-B1, Glu-D1, which code for high molecular weight subunits of glutenin in hexaploid wheat. Cereal Research Communications, 11, 29–35.
Payne P I, Nightingale M A, Krattiger A F, Holt L M. 1987. The relationship between HMW glutenin subunit composition and the bread-making quality of British-grown wheat varieties. Journal of the Science of Food & Agriculture, 40, 51–65.
Ram S, Shoran J, Mishra B. 2007. Nap Hal, an Indian landrace of wheat, contains unique genes for better biscuit making quality. Journal of Plant Biochemistry & Biotechnology, 16, 83–86.
Rasheed A, Xia X, Yan Y, Appels R, Mahmood T, He Z. 2014. Wheat seed storage proteins: Advances in molecular genetics, diversity and breeding applications. Journal of Cereal Science, 60, 11–24.
Seilmeier W, Belitz H D, Wieser H. 1991. Separation and quantitative determination of high-molecular-weight subunits of glutenin from different wheat varieties and genetic variants of the variety Sicco. European Food Research and Technology, 192, 124–129.
Shewry P R , Halford N G. 2002. Cereal seed storage proteins: Structures, properties and role in grain utilization. Journal of Experimental Botany, 53, 947–958.
Shewry P R, Halford N G, Tatham A S. 1992. High molecular weight subunits of wheat glutenin. Journal of Cereal Science, 15, 105–120.
Shewry P R, Tatham A S. 1990. The prolamin storage proteins of cereal seeds: Structure and evolution. Biochemical Journal, 267, 1–12.
Tian J C. 2006. Theroy and Method of Cereal Quality Measurement. Science Press, Beijing. p. 112. (in Chinese)
Uthayakumaran S, Lukow O M, Jordan M C, Cloutier S. 2003. Development of genetically modified wheat to assess its dough functional properties. Molecular Breeding, 11, 249–258.
Wieser H, Kieffer R. 2001. Correlations of the amount of gluten protein types to the technological properties of wheat flours determined on a micro-scale. Journal of Cereal Science, 34, 19–27.
Wrigley C W, Asenstorfer R, Batey I L, Cornish G B, Day L, Mares D, Mrva K. 2009. The biochemical and molecular basis of wheat quality. In: Carver B F, ed., Wheat Science and Trade. Wiley-Blackwell, Ames. pp. 495–520.
Wrigley C W, Bekes F, Bushuk W. 2006. Gliadin and glutenin: The unique balance of wheat quality. International Association of Cereal Chemists, St. Paul, MN.
Yang Y S, Li S M, Zhang K P, Dong Z Y, Li Y W, An X L, Chen J, Chen Q F, Jiao Z, Liu X, Qin H J, Wang D W. 2014. Efficient isolation of ion beam-induced mutants for homoeologous loci in common wheat and comparison of the contributions of Glu-1 loci to gluten functionality. Theoretical and Applied Genetics, 127, 359–372.
Zhang P P, Jondiko T O, Tilley M, Awika J M. 2014. Effect of high molecular weight glutenin subunit composition in common wheat on dough properties and steamed bread quality. Journal of the Science of Food & Agriculture, 94, 2801–2806.
Zhang P P, Ma H X, Yao J B, Awika J M. 2015. Effects of Glu-1 deletion on size distribution of glutenin polymeric protein and dough properties in common wheat. Acta Agronomica Sinica, 41, 22–30. (in Chinese)
Zhang X, Zhang B Q, Wu H Y, Lu C B, Lv G F, Liu D T, Jiang M, Song G H, Gao D R. 2018. Effect of high-molecular-weight glutenin subunit deletion on soft wheat quality properties and sugar-snap cookie quality estimated through near-isogenic lines. Journal of Integrative Agriculture, 17, 1066–1073.
Zhu J T, Hao P C, Chen G X, Han C X, Li X H, Zeller F J, Hsam S L, Hu Y K, Yan Y M. 2014. Molecular cloning, phylogenetic analysis, and expression profiling of endoplasmic reticulum molecular chaperone BiP genes from bread wheat (Triticum aestivum L.). BMC Plant Biology, 14, 260.
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