000			03479nab a22004577a 4500
001			G90240
003			MX-TxCIM
005			20230912212610.0
008			210702b2007 xxc|||p|op||| 00| 0 eng d
022			_a1480-3321 (Online)
022			_a0831-2796
024	8		_ahttps://doi.org/10.1139/G07-089
040			_aMX-TxCIM
041			_aeng
090			_aCIS-5157
100	0		_aXiaohui Li _918575
245	1	0	_aMolecular cloning, heterologous expression, and phylogenetic analysis of a novel y-type HMW glutenin subunit gene from the G genome of Triticum timopheevi
260			_aOntario (Canada) : _bCanadian Science Publishing, _c2007.
340			_aPrinted|Computer File
500			_aPeer review
500			_aPeer-review: Yes - Open Access: Yes|http://science.thomsonreuters.com/cgi-bin/jrnlst/jlresults.cgi?PC=MASTER&ISSN=0831-2796
520			_aA 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.
536			_aGlobal Wheat Program
546			_aText in English
594			_aINT2411
650		7	_aWheat _2AGROVOC _91310
650		7	_aGlutenins _2AGROVOC _91137
650		7	_aTriticum timopheevii _2AGROVOC _931621
650		7	_aGenomes _2AGROVOC _91131
700	0		_aZhang Yan-zhen _920781
700	0		_aLiyan Gao _920798
700	0		_aAili Wang _920799
700	0		_aKangmin Ji _920800
700	1		_aHe Zhonghu _gGlobal Wheat Program _8INT2411 _9838
700	1		_91980 _aAppels, R.
700	0		_91979 _aWujun Ma
700	0		_915752 _aYueming Yan
773	0		_tGenome _n635005 _gv. 50, no. 12, p. 1130-1140 _dOntario (Canada) : Canadian Science Publishing, 2007. _wG444552 _x0831-2796
856	4		_yAccess only for CIMMYT Staff _uhttps://hdl.handle.net/20.500.12665/649
942			_cJA _2ddc _n0
999			_c26918 _d26918