TY  - JA
AU  - Xiaohui Li
AU  - Zhang Yan-zhen
AU  - Liyan Gao
AU  - Aili Wang
AU  - Kangmin Ji
AU  - He Zhonghu
AU  - Appels,R.
AU  - Wujun Ma
AU  - Yueming Yan
TI  - Molecular cloning, heterologous expression, and phylogenetic analysis of a novel y-type HMW glutenin subunit gene from the G genome of Triticum timopheevi
SN  - 1480-3321
PY  - 2007///
CY  - Ontario (Canada)
PB  - Canadian Science Publishing
KW  - Wheat
KW  - AGROVOC
KW  - Glutenins
KW  - Triticum timopheevii
KW  - Genomes
N1  - Peer review; Peer-review: Yes - Open Access: Yes|http://science.thomsonreuters.com/cgi-bin/jrnlst/jlresults.cgi?PC=MASTER&ISSN=0831-2796
N2  - A novel y-type high molecular weight (HMW) glutenin subunit gene from the G genome of Triticum timopheevi (2n = 4x = 28, AAGG) was isolated and characterized. Genomic DNA from accession CWI17006 was amplified and a 2200 bp fragment was obtained. Sequence analysis revealed a complete open reading frame including N- and C-terminal ends and a central repetitive domain encoding 565 amino acid residues. The molecular weight of the deduced subunit was 77 031, close to that of the x-type glutenin subunits. Its mature protein structure, however, demonstrated that it was a typical y-type HMW subunit. To our knowledge, this is the largest y-type subunit gene among Triticum genomes. The molecular structure and phylogenetic analysis assigned it to the G genome and it is the first characterized y-type HMW glutenin subunit gene from T. timopheevi. Comparative analysis and secondary structure prediction showed that the subunit possessed some unique characters, especially 2 large insertions of 45 (6 hexapeptides and a nonapeptide) and 12 (2 hexapeptides) amino acid residues that mainly contributed to its higher molecular weight and allowed more coils to be formed in its tertiary structure. Additionally, more α-helixes in the repeat domain of the subunit were found when compared with 3 other y-type subunits. We speculate that these structural characteristics improve the formation of gluten polymer. The novel subunit, expressed as a fusion protein in E. coli, moved more slowly in SDS–PAGE than the subunit Bx7, so it was designated Gy7*. As indicated in previous studies, increased size and more numerous coils and α-helixes of the repetitive domain might enhance the functional properties of HMW glutenins. Consequently, the novel Gy7* gene could have greater potential for improving wheat quality
UR  - https://hdl.handle.net/20.500.12665/649
DO  - https://doi.org/10.1139/G07-089
T2  - Genome
ER  -