1Mx2.1, a novel high-molecular-weight glutenin subunit from Aegilops comosa and its relationship to high-quality dough

2019 ◽  
Vol 17 (04) ◽  
pp. 379-381
Author(s):  
Xuye Du ◽  
Biya Xia ◽  
Fang He ◽  
Mingjian Ren
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Genetic Resource ◽  
Cysteine Residue ◽  
Glutenin Subunit ◽  
Repetitive Domain ◽  
Aegilops Comosa ◽  
Dough Quality

AbstractHigh-molecular-weight glutenin subunit (HMW-GS) of endosperm is mainly correlated with dough quality of bread wheat. In wheat cultivars, the HMW-GS genes with good processing quality are limited. However, there are an amount of excellent HMW-GS genes presenting in wheat-related species. In this work, two novel HMW-GS genes located on 1 M chromosome from Aegilops comosa have been cloned, designated as 1Mx2.1 and 1My12.1, respectively. The molecular structure of 1Mx2.1 and 1My12.1 showed high similarity with the published HMW-GS, but containing unique structures. 1Mx2.1 contained an extra cysteine residue in the repetitive domain, and 1My12.1 lost the conservative cysteine residue in the C-terminal domain. In vitro mixing test has indicated that 1Mx2.1 contributes excellent dough quality. The Ae. comosa can be used as an important genetic resource for wheat quality improvement.

Modification of a novel x-type high-molecular-weight glutenin subunit gene from Aegilops markgrafii to improve dough strength of wheat flour

2018 ◽  
Vol 69 (9) ◽  
pp. 873
Author(s):  
Xin Ma ◽  
Xuye Du ◽  
Cunyao Bo ◽  
Hongwei Wang ◽  
Anfei Li ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Wheat Flour ◽  
Cysteine Residue ◽  
Site Directed Mutagenesis ◽  
Cysteine Residues ◽  
Dough Strength ◽  
Typical Structure ◽  
Dough Quality

High-molecular-weight glutenin subunits (HMW-GS) in bread wheat are major determinants of dough viscoelastic properties and the end-use quality of wheat flour. Cysteine residues, which form intermolecular disulphide bonds in HMW-GS, could improve the strength of gluten. To our knowledge, the number and position of cysteine residues in HMW-GS are conserved between wheat (Triticum aestivum) and Aegilops markgrafii. In the present study, we modified a gene (1Cx1.1) from Ae. markgrafii for an HMW-GS that possessed the typical structure and conserved number of cysteines. Site-directed mutagenesis was carried out in 1Cx1.1 to investigate how the position of cysteine residues in HMW-GS affects the mixing properties of dough. Six HMW-GS containing an extra cysteine residue were expressed in Escherichia coli, and the proteins were purified at sufficient scale for incorporation into flour to test dough quality. There were large differences in dough property among samples containing different modified subunits. Cysteine substituting in the N-terminal or repetitive-domain of HMW-GS could significantly improve dough quality. The results showed that the strategy was useful for providing genetic resources for gene engineering, and hence could be valuable for improving the processing quality of wheat.

Cloning and functional analysis of a novel x-type high-molecular-weight glutenin subunit with altered cysteine residues from Aegilops umbellulata

2017 ◽  
Vol 68 (5) ◽  
pp. 409 ◽  
Author(s):  
Wenqian Hou ◽  
Wei Feng ◽  
Guanghui Yu ◽  
Xuye Du ◽  
Mingjian Ren
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Triticum Aestivum L ◽  
Positive Control ◽  
Cysteine Residue ◽  
Glutenin Subunit ◽  
Wheat Varieties ◽  
Reading Frame ◽  
Aegilops Umbellulata ◽  
Dough Quality

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.

Adsorption of the High Molecular Weight Glutenin Subunit 1Dx5 Compared to the 58-kDa Central Repetitive Domain and α-gliadins

2001 ◽  
Vol 34 (2) ◽  
pp. 141-150 ◽  
Author(s):  
J. Örnebro ◽  
T. Nylander ◽  
A.-C. Eliasson ◽  
P.R. Shewry ◽  
A.S. Tatham ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Glutenin Subunit ◽  
Repetitive Domain

The behaviour of the high molecular-weight glutenin subunit 1Dx5, the 58 kDa central repetitive domain and α-gliadins at the air–aqueous interface

2003 ◽  
Vol 38 (2) ◽  
pp. 147-156 ◽  
Author(s):  
J. Örnebro ◽  
T. Nylander ◽  
A.-C. Eliasson ◽  
P.R. Shewry ◽  
A.S. Tatham ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Glutenin Subunit ◽  
Repetitive Domain

A cysteine in the repetitive domain of a high-molecular-weight glutenin subunit interferes with the mixing properties of wheat dough

Amino Acids ◽  
2012 ◽  
Vol 44 (3) ◽  
pp. 1061-1071 ◽  
Author(s):  
Xin Gao ◽  
Qisen Zhang ◽  
Marcus P. Newberry ◽  
Ken J. Chalmers ◽  
Diane E. Mather
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Glutenin Subunit ◽  
Repetitive Domain ◽  
Mixing Properties ◽  
Wheat Dough

scholarly journals Characterisation of a novel high-molecular-weight glutenin subunit 1Dy12.3 from hexaploid wheat (Triticum aestivum L.)

2012 ◽  
Vol 48 (No. 4) ◽  
pp. 157-168 ◽  
Author(s):  
D. Mihálik ◽  
E. Gregová ◽  
P. Galuszka ◽  
L. Ohnoutková ◽  
T. Klempová ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Triticum Aestivum ◽  
High Molecular Weight ◽  
Hexaploid Wheat ◽  
Signal Sequence ◽  
Triticum Aestivum L ◽  
Glutenin Subunit ◽  
Repetitive Domain ◽  
Sds Page ◽  
Methionine Residues

A novel high-molecular-weight glutenin subunit encoded by the Glu-1D locus was identified in hexaploid wheat (Triticum aestivum L.) cultivar Noe and was designated as 1Dy12.3. This subunit differed in SDS-PAGE mobility from the well-known 1Dy10 and 1Dy12 subunits that are also encoded by this locus. An analysis of the gene sequences confirmed the uniqueness of 1Dy12.3 and revealed that it is most closely related to the 1Dy12 subunit. The size of the deduced protein was calculated to be 67 884 Da, which is different from the 1Dy10 and 1Dy12 subunits (67 475 Da and 68 713 Da, respectively). The 1Dy12.3 protein consists of 652 residues, with a highly conserved signal sequence and N- and C-terminal domains, although the central repetitive domain comprising motifs of hexapeptide (PGQGQQ) and nonapeptide (GYYPTSLQQ) repeats was less conserved. The 1Dy12.3 subunit demonstrates fewer QHPEQG hexapeptide motifs and exhibits an increased number of methionine residues in comparison to the other characterised high-molecular-weight glutenin subunits. The 1Dy12.3 subunit was cloned and expressed in Escherichia coli and was detected with a prolamin-specific antibody. The size of the detected immunocomplex corresponded to the native 1Dy12.3 protein isolated from grains. The existence and characterisation of this novel high-molecular-weight glutenin subunit increases the diversity of the glutenins encoded by the Glu-1D locus.

Expression and Functional Analysis ofMr58 000 Peptides Derived from the Repetitive Domain of High Molecular Weight Glutenin Subunit 1Dx5

1998 ◽  
Vol 27 (3) ◽  
pp. 209-215 ◽  
Author(s):  
F. Buonocore ◽  
L. Bertini ◽  
C. Ronchi ◽  
F. Békés ◽  
C. Caporale ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Functional Analysis ◽  
High Molecular Weight ◽  
Glutenin Subunit ◽  
Repetitive Domain
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