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

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

Synergistic and Additive Effects of Three High Molecular Weight Glutenin Subunit Loci. II. Effects on Wheat Dough Functionality and End-Use Quality

2002 ◽  
Vol 79 (2) ◽  
pp. 301-307 ◽  
Author(s):  
H. L. Beasley ◽  
S. Uthayakumaran ◽  
F. L. Stoddard ◽  
S. J. Partridge ◽  
L. Daqiq ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Glutenin Subunit ◽  
Additive Effects ◽  
Wheat Dough ◽  
End Use ◽  
Dough Functionality

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.

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.

Synergistic and Additive Effects of Three High Molecular Weight Glutenin Subunit Loci. I. Effects on Wheat Dough Rheology

2002 ◽  
Vol 79 (2) ◽  
pp. 294-300 ◽  
Author(s):  
S. Uthayakumaran ◽  
H. L. Beasley ◽  
F. L. Stoddard ◽  
M. Keentok ◽  
N. Phan-Thien ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Glutenin Subunit ◽  
Dough Rheology ◽  
Additive Effects ◽  
Wheat Dough
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