Identification and molecular characterization of a novel y-type Glu-D t  1 glutenin gene of Aegilops tauschii

Yan, Yueming; Zheng, Ji-Gang; Xiao, Yinghua; Yu, Jing; Hu, Yingkao; Cai, Minhua; Li, Y.; Hsam, S. L. K.; Zeller, F. J.

doi:10.1007/s00122-003-1547-y

Cited by 55 publications

(36 citation statements)

References 42 publications

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“…The N-termini of x-type subunits are composed of 86-89 residues, while those of y-type subunits are typically 104-105 residues. The C-termini of all subunits are composed of 42 residues and the central repetitive domain comprises 630-830 residues and mainly contributes to the differences between all the subunits (Sun et al 2004;Yan et al 2004).…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning of a novel chimeric HMW glutenin subunit gene 1Dx5′ from a common wheat line W958

Feng

et al. 2010

Mol Breeding

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A novel chimeric high-molecular-weight (HMW) glutenin subunit gene from a new common wheat line W958 (2n = 6x = 42) was isolated and characterized. SDS-PAGE analysis revealed that this glutenin subunit has similar electrophoretic mobility to 1Dx5, so it was designated 1Dx5 0 . Genomic DNA from W958 was amplified and a 2,505-bp fragment was obtained. The 1Dx5 0 subunit showed a chimeric primary structure of 1Dx5 and 1Dx2, with the 1Dx5 sequence in the 5 0 and middle repetitive regions and the 1Dx2 sequence in the repetitive domain and 3 0 region. MALDI-TOF-MS analysis demonstrated that 1Dx5 0 had a molecular weight of 86815.1 Da, close to that of an x-type glutenin subunit. Secondary structure analysis showed that this subunit had six helixes and one strand, including four helixes in the repetitive domain which could enhance the dough properties. Additionally, the promoter of 1Dx5 0 was obtained and showed the same sequence as 1Dx5 or 1Dx2 except for a few base conversions. The promoter analysis indicated that the cis-acting regulatory elements of 1Dx5 0 were the same as those of 1Dx5 and/or 1Dx2. Previously, we have demonstrated that this novel glutenin subunit is associated with good bread-making quality and comprises a very large proportion of the F2 segregation population.Electronic supplementary material The online version of this article

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Section: Introductionmentioning

confidence: 99%

Molecular cloning of a novel chimeric HMW glutenin subunit gene 1Dx5′ from a common wheat line W958

Feng

et al. 2010

Mol Breeding

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“…et Migush (GenBank: AY695379, Jiang et al 2006). However, the genes for the 1Dy subunits originating from diploid ancestors possess much higher variation in comparison to those isolated from hexaploid wheat varieties (Mackie et al 1996;Dvorak et al 1998;Gianibelli & Solomon 2003;Yan et al 2004;Fang et al 2009;Xu et al 2010). Nevertheless, wheat breeders prefer to use more-related genomes as the donors for the improvement of bread wheat.…”

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confidence: 99%

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

Mihálik¹,

Gregová²,

Galuszka³

et al. 2012

CZECH J GENET PLANT

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Abstract: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.

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“…tauschii have been characterized (Wan et al 2005). Evidence from molecular analysis demonstrated that the HMW glutenin subunits from wheat and related species have highly conserved structures, consisting of a signal peptide (21 residues), an N-terminal domain (86-89 residues in x-type and 104 in y-type subunits), a C-terminal domain (42 residues), and a central repetitive domain (630-830 residues) that is mainly responsible for differences in molecular weight of the subunits Wan et al 2002Wan et al , 2005Yan et al 2004;Sun et al 2006;Zhang et al 2006). The HMW glutenin genes, therefore, could derive from a common ancestor.…”

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confidence: 99%

Novel x-Type High-Molecular-Weight Glutenin Genes From Aegilops tauschii and Their Implications on the Wheat Origin and Evolution Mechanism of Glu-D1-1 Proteins

Zhang

Wang

et al. 2008

Genetics

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Two new x-type high-molecular-weight glutenin subunits with similar size to 1Dx5, designated 1Dx5 *t and 1Dx5.1 *t in Aegilops tauschii, were identified by SDS-PAGE, RP-HPLC, and MALDI-TOF-MS. The coding sequences were isolated by AS-PCR and the complete ORFs were obtained. Allele 1Dx5 *t consists of 2481 bp encoding a mature protein of 827 residues with deduced M r of 85,782 Da whereas 1Dx5.1 *t comprises 2526 bp encoding 842 residues with M r of 87,663 Da. The deduced M r 's of both genes were consistent with those determined by MALDI-TOF-MS. Molecular structure analysis showed that the repeat motifs of 1Dx5 *t were correspondingly closer to the consensus compared to 1Dx5.1 *t and 1Dx5 subunits. A total of 11 SNPs (3 in 1Dx5 *t and 8 in 1Dx5.1 *t ) and two indels in 1Dx5 *t were identified, among which 8 SNPs were due to C-Tor A-G transitions (an average of 73%). Expression of the cloned ORFs and N-terminal sequencing confirmed the authenticities of the two genes. Interestingly, several hybrid clones of 1Dx5 *t expressed a slightly smaller protein relative to the authentic subunit present in seed proteins; this was confirmed to result from a deletion of 180 bp through illegitimate recombination as well as an in-frame stop codon. Network analysis demonstrated that 1Dx5 *t , 1Dx2 t , 1Dx1.6 t , and 1Dx2.2 * represent a root within a network and correspond to the common ancestors of the other Glu-D-1-1 alleles in an associated star-like phylogeny, suggesting that there were at least four independent origins of hexaploid wheat. In addition to unequal homologous recombination, duplication and deletion of large fragments occurring in Glu-D-1-1 alleles were attributed to illegitimate recombination.

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Identification and molecular characterization of a novel y-type Glu-D t 1 glutenin gene of Aegilops tauschii

Cited by 55 publications

References 42 publications

Molecular cloning of a novel chimeric HMW glutenin subunit gene 1Dx5′ from a common wheat line W958

Molecular cloning of a novel chimeric HMW glutenin subunit gene 1Dx5′ from a common wheat line W958

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

Novel x-Type High-Molecular-Weight Glutenin Genes From Aegilops tauschii and Their Implications on the Wheat Origin and Evolution Mechanism of Glu-D1-1 Proteins

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