Cloning and functional analysis of a novel x-type high-molecular-weight glutenin subunit with altered cysteine residues from Aegilops umbellulata
Wenqian Hou A , Wei Feng A , Guanghui Yu B , Xuye Du A D and Mingjian Ren C D
+ Author Affiliations
- Author Affiliations
A College of Life Sciences, Guizhou Normal University, No. 116 Baoshan North Street, Guiyang, 550001, Guizhou Province, China P.R.
B College of Resources and Environmental Sciences, China Agricultural University, No. 2 Yuanmingyuan West Road, Beijing, 100193, China P.R.
C College of Agronomy, Guizhou Sub-center of National Wheat Improvement Center, Guizhou University, No. 82 Huaxi Avenue, Guiyang, 550001, Guizhou Province, China P.R.
D Corresponding authors. Emails: duxuye@163.com; rmj@163.com
Crop and Pasture Science 68(5) 409-414 https://doi.org/10.1071/CP17113
Submitted: 9 March 2017 Accepted: 13 April 2017 Published: 24 May 2017
Abstract
In common wheat (Triticum aestivum L.) and its relative species, considerable progress has been made in understanding the structure and function of the high-molecular-weight glutenin subunit (HMW-GS). As a species closely related to wheat, Aegilops umbellulata is an important resource for wheat genetic improvement. In this paper, we report a novel HMW-GS 1Ux3.5 in Aegilops umbellulata Y361. The complete open reading frame (ORF) coding for 1Ux3.5 was cloned and sequenced. Analysis of the deduced amino acid sequence revealed that the primary structure of 1Ux3.5 was similar to those of previously published HMW-GSs. The 1Ux3.5 possessed an extra cysteine residue in the repetitive domain, indicating that the subunit may be related to excellent dough quality. Subsequently, the single proteins of 1Ux3.5 and 1Dx5 (used as positive control) were purified at a scale sufficient for incorporation into flour for a dough quality test. Both the SDS sedimentation volume and mixograph parameters demonstrated that 1Ux3.5 showed a greater contribution to the dough quality than 1Dx5. Therefore, the 1Ux3.5 subunit from Aegilops umbellulata may have potential value in improving the processing properties of hexaploid wheat varieties.
Additional keywords: in vitro analysis, processing quality, storage protein, U genome.
References
Bansal M, Kaur S, Dhaliwal HS, Bains NS, Bariana HS, Chhuneja P, Bansal UK (2017) Mapping of Aegilops umbellulata-derived leaf rust and stripe rust resistance loci in wheat. Plant Pathology 66, 38–44.| Mapping of Aegilops umbellulata-derived leaf rust and stripe rust resistance loci in wheat.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC28XitVGntr%2FN&md5=2c666298ac19e8e766d5736c485d39dbCAS |
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.
| Diversity of grain protein and bread wheat quality: II. Correlation between high molecular weight subunits of glutenin and flour quality characteristics.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL2MXmtFeks78%3D&md5=b65846d91e13ff7d14cc65065c9cb098CAS |
Chen FG, Liu SW, Zhao F, Xu CH, Xia GM (2010) Molecular characterisation of the low-molecular weight glutenin subunit genes of tall wheatgrass and functional properties of one clone Ee34. Amino Acids 38, 991–999.
| Molecular characterisation of the low-molecular weight glutenin subunit genes of tall wheatgrass and functional properties of one clone Ee34.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXkt12qs7k%3D&md5=9fb9963ef72ef75f52cba7ab1c536929CAS |
Dai SF, Zhao L, Xue XF, Jia YN, Liu DC, Pu ZJ, Zheng YL, Yan ZH (2015) Analysis of high-molecular-weight glutenin subunits in five amphidiploids and their parental diploid species Aegilops umbellulata and Aegilops uniaristata. Plant Genetic Resources 13, 186–189.
| Analysis of high-molecular-weight glutenin subunits in five amphidiploids and their parental diploid species Aegilops umbellulata and Aegilops uniaristata.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC2MXhtFyls7vE&md5=8cbb02d74669e71099d2ee68c7bbe7fcCAS |
Don C, Lichtendonk WJ, Plijter JJ, Hamer RJ (2003) Understanding the link between GMP and dough: from glutenin particles in flour towards developed dough. Journal of Cereal Science 38, 157–165.
| Understanding the link between GMP and dough: from glutenin particles in flour towards developed dough.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXls1ertLo%3D&md5=cd69a6b5ba14c001bdbfd9a50eb9d586CAS |
Du XY, Zhang XC (2016) Molecular cloning and functional characterization of two novel high-molecular-weight glutenin subunit genes in Aegilops markgrafii. Journal of Genetics In press
Edae EA, Olivera PD, Jin Y, Poland JA, Rouse MN (2016) Genotype-by-sequencing facilitates genetic mapping of a stem rust resistance locus in Aegilops umbellulata, a wild relative of cultivated wheat. BMC Genomics 17, 1039
| Genotype-by-sequencing facilitates genetic mapping of a stem rust resistance locus in Aegilops umbellulata, a wild relative of cultivated wheat.Crossref | GoogleScholarGoogle Scholar |
Gao X, Zhang QS, Newberry MP, Chalmers KJ, Mather DE (2013) A cysteine in the repetitive domain of a high-molecular-weight glutenin subunit interferes with the mixing properties of wheat dough. Amino Acids 44, 1061–1071.
| A cysteine in the repetitive domain of a high-molecular-weight glutenin subunit interferes with the mixing properties of wheat dough.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3sXitlChs7Y%3D&md5=2f27f866ec2bc7f6215f31801d6c7a8bCAS |
Gianibelli MC, Larroque OR, MacRitchie F, Wrigley CW (2001) Biochemical, genetic, and molecular characterization of wheat endosperm proteins. Cereal Chemistry 78, 635–646.
| Biochemical, genetic, and molecular characterization of wheat endosperm proteins.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXosVKmtrg%3D&md5=c3e5e4163ab3ffc75d098cf8c058e98bCAS |
Jiang QT, Zhang XW, Ma J, Wei L, Zhao S, Zhao QZ, Qi PF, Lu ZX, Zheng YL, Wei YM (2014) Characterization of high-molecular-weight glutenin subunits from Eremopyrum bonaepartis and identification of a novel variant with unusual high molecular weight and altered cysteine residues. Planta 239, 865–875.
| Characterization of high-molecular-weight glutenin subunits from Eremopyrum bonaepartis and identification of a novel variant with unusual high molecular weight and altered cysteine residues.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC2cXivVKqsg%3D%3D&md5=01cfc72c93b4978066d17fa83724563eCAS |
Lafiandra D, D’Ovidio R, Porceddu E, Margiotta B, Colaprico G (1993) New data supporting high Mr glutenin subunit 5 as determinant of quality differences among the pairs 5+10 vs 2+12. Journal of Cereal Science 18, 197–205.
| New data supporting high Mr glutenin subunit 5 as determinant of quality differences among the pairs 5+10 vs 2+12.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2cXis1ylur4%3D&md5=0b6696b035d6f731aa2ff62f61c10633CAS |
Lawrence GJ, Shepherd KW (1981) Chromosomal location of genes controlling seed proteins in species related to wheat. Theoretical and Applied Genetics 59, 25–31.
Liu ZJ, Yan ZH, Wan YF, Liu KF, Zheng YF, Wang DW (2003) Analysis of HMW glutenin subunits and their coding sequences in two diploid Aegilops species. Theoretical and Applied Genetics 106, 1368–1378.
| Analysis of HMW glutenin subunits and their coding sequences in two diploid Aegilops species.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXjslamsr8%3D&md5=de756da2c7e9d6580ef2fd7aeb34cbe3CAS |
Liu SW, Zhao F, Gao X, Chen FG, Xia GM (2010) A novel high molecular weight glutenin subunit from Australopyrum retrofractum. Amino Acids 39, 385–392.
| A novel high molecular weight glutenin subunit from Australopyrum retrofractum.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXotVais7s%3D&md5=8d1abd141c4369db65880e58e980a64bCAS |
Masci S, D’Ovidio R, Lafiandra D, Kasarda DD (1998) Characterization of a low-molecular-weight glutenin subunit gene from bread wheat and the corresponding protein that represents a major subunit of the glutenin polymer. Plant Physiology 118, 1147–1158.
| Characterization of a low-molecular-weight glutenin subunit gene from bread wheat and the corresponding protein that represents a major subunit of the glutenin polymer.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK1MXnsQ%3D%3D&md5=8b38d848000e20c7a0a3eea06dac1f7cCAS |
Masci S, Rovelli L, Kasarda DD, Vensel WH, Lafiandra D (2002) Characterisation and chromosomal localisation of C-type low-molecular-weight glutenin subunits in the bread wheat cultivar Chinese Spring. Theoretical and Applied Genetics 104, 422–428.
| Characterisation and chromosomal localisation of C-type low-molecular-weight glutenin subunits in the bread wheat cultivar Chinese Spring.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XislOgt70%3D&md5=5961d9235e45138e27fb2a326fbf43fdCAS |
Murray MG, Thompson WF (1980) Rapid isolation of high molecular weight plant DNA. Nucleic Acids Research 8, 4321–4326.
| Rapid isolation of high molecular weight plant DNA.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL3cXmtVSmtL8%3D&md5=3f8e0a46f706199e76ffa41fe17e604aCAS |
Özgen M, Birsin MA, Benlioglu B (2017) Biotechnological characterization of a diverse set of wheat progenitors (Aegilops sp. and Triticum sp.) using callus culture parameters. Plant Genetic Resources 15, 45–50.
| Biotechnological characterization of a diverse set of wheat progenitors (Aegilops sp. and Triticum sp.) using callus culture parameters.Crossref | GoogleScholarGoogle Scholar |
Payne PI, Holt LM, Krattiger AF, Carrillo JW (1988) Relationships between seed quality characteristics and HMW glutenin subunit composition determined using wheats grown in Spain. Journal of Cereal Science 7, 229–235.
| Relationships between seed quality characteristics and HMW glutenin subunit composition determined using wheats grown in Spain.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL1cXksFWrtbs%3D&md5=514150e723ff5aca3de87efa752f7920CAS |
Shewry PR, Napier JA, Tatham AS (1995) Seed storage proteins: structures and biosynthesis. The Plant Cell 7, 945–956.
| Seed storage proteins: structures and biosynthesis.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2MXnt1Sgtrk%3D&md5=25503092d221664ff08ba785fddbe7d0CAS |
Shewry PR, Gilbert SM, Savage AWJ, Tatham AS, Wan YF, Belton PS, Wellner N, D’Ovidio R, Bekes F, Halford NG (2003) Sequence and properties of HMW subunit 1Bx20 from pasta wheat (Triticum durum) which is associated with poor end use properties. Theoretical and Applied Genetics 106, 744–750.
| Sequence and properties of HMW subunit 1Bx20 from pasta wheat (Triticum durum) which is associated with poor end use properties.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXhsVSls70%3D&md5=98e192f1dd60043009dd2b1ccd4f517cCAS |
Wan YF, Wang DW, Shewry PR, Halford NG (2002) Isolation and characterization of five novel high molecular weight subunit of glutenin genes from Triticum timopheevi and Aegilops cylindrical. Theoretical and Applied Genetics 104, 828–839.
| Isolation and characterization of five novel high molecular weight subunit of glutenin genes from Triticum timopheevi and Aegilops cylindrical.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XktlWnt7w%3D&md5=9fc94c4705a20487f6c770f90f9bae20CAS |
Wieser H (2007) Chemistry of gluten proteins. Food Microbiology 24, 115–119.
| Chemistry of gluten proteins.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28XhtVagtLnM&md5=cc65f53fa5ff3a61d0a85cfb98734a30CAS |
