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Isolation and characterization of a novel variant of HMW glutenin subunit gene from the St genome of Pseudoroegneria stipifolia
Li, Z. X.1,3; Zhang, X. Q.1; Zhang, H. G.1,2; Cao, S. H.1; Wang, D. W.1; Hao, S. T.1; Li, L. H.4; Li, H. J.4; Wang, X. P.1
2008-05-01
发表期刊JOURNAL OF CEREAL SCIENCE
卷号47期号:3页码:429-437
文章类型Article
摘要The x- and y-type high molecular weight (HMW) glutenin subunits are conserved seed storage proteins in wheat and related species. Here we describe investigations on the HMW glutenin subunits from several Pseudoroegneria accessions. The electrophoretic mobilities of the HMW glutenin subunits from Pd. stipifolia, Pd tauri and Pd strigosa were much faster than those of orthologous wheat subunits, indicating that their protein size may be smaller than that of wheat subunits. The coding sequence of the Glu-1St1 subunit (encoded by the Pseudoroegneria stipifolia accession PI325181) was isolated, and found to represent the native open reading frame (ORF) by in vitro expression. The deduced amino acid sequence of Glu-1St1 matched with that determined from the native subunit by mass spectrometric analysis. The domain organization in Glu-1St1 showed high similarity with that of typical HMW glutenin subunits. However, Glu-1St1 exhibited several distinct characteristics. First, the length of its repetitive domain was substantially smaller than that of conventional subunits, which explains its much faster electrophoretic mobility in SDS-PAGE. Second, although the N-terminal domain of Glu-1St1 resembled that of y-type subunit, its C-terminal domain was more similar to that of x-type subunit. Third, the N- and C-terminat domains of Glu-1St1 shared conserved features with those of barley D-hordein, but the repeat motifs and the organization of its repetitive domain were more similar to those of HMW glutenin subunits than to D-hordein. We conclude that Glu-1St1 is a novel variant of HMW glutenin subunits. The analysis of Glu-1St1 may provide new insight into the evolution of HMW glutenin subunits in Triticeae species. (C) 2007 Elsevier Ltd. All rights reserved.; The x- and y-type high molecular weight (HMW) glutenin subunits are conserved seed storage proteins in wheat and related species. Here we describe investigations on the HMW glutenin subunits from several Pseudoroegneria accessions. The electrophoretic mobilities of the HMW glutenin subunits from Pd. stipifolia, Pd tauri and Pd strigosa were much faster than those of orthologous wheat subunits, indicating that their protein size may be smaller than that of wheat subunits. The coding sequence of the Glu-1St1 subunit (encoded by the Pseudoroegneria stipifolia accession PI325181) was isolated, and found to represent the native open reading frame (ORF) by in vitro expression. The deduced amino acid sequence of Glu-1St1 matched with that determined from the native subunit by mass spectrometric analysis. The domain organization in Glu-1St1 showed high similarity with that of typical HMW glutenin subunits. However, Glu-1St1 exhibited several distinct characteristics. First, the length of its repetitive domain was substantially smaller than that of conventional subunits, which explains its much faster electrophoretic mobility in SDS-PAGE. Second, although the N-terminal domain of Glu-1St1 resembled that of y-type subunit, its C-terminal domain was more similar to that of x-type subunit. Third, the N- and C-terminat domains of Glu-1St1 shared conserved features with those of barley D-hordein, but the repeat motifs and the organization of its repetitive domain were more similar to those of HMW glutenin subunits than to D-hordein. We conclude that Glu-1St1 is a novel variant of HMW glutenin subunits. The analysis of Glu-1St1 may provide new insight into the evolution of HMW glutenin subunits in Triticeae species. (C) 2007 Elsevier Ltd. All rights reserved.
关键词Pseudoroegneria Stipifolia Hmw Glutenin Subunit D-hordein Wheat Phylogenetic Analysis Evolution
WOS标题词Science & Technology ; Life Sciences & Biomedicine
学科领域生物科学
关键词[WOS]DESORPTION/IONISATION MASS-SPECTROMETRY ; MOLECULAR-WEIGHT GLUTENIN ; STORAGE PROTEINS ; WHEAT ; REGIONS ; IDENTIFICATION ; SEQUENCE ; ALLELES ; BARLEY ; LOCUS
收录类别SCI
语种英语
WOS研究方向Food Science & Technology
WOS类目Food Science & Technology
WOS记录号WOS:000256601200005
引用统计
被引频次:14[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://210.75.249.4/handle/363003/1210
专题中国科学院西北高原生物研究所
作者单位1.Chinese Acad Sci, Inst Genet & Dev Biol, State Key Lab Plant Cell & Chromosome Engn, Beijing 100101, Peoples R China
2.Chinese Acad Sci, NW Inst Plateau Biol, Xining 810008, Peoples R China
3.Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China
4.Chinese Acad Agr Sci, Inst Crop Sci, Beijing 100081, Peoples R China
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Li, Z. X.,Zhang, X. Q.,Zhang, H. G.,et al. Isolation and characterization of a novel variant of HMW glutenin subunit gene from the St genome of Pseudoroegneria stipifolia[J]. JOURNAL OF CEREAL SCIENCE,2008,47(3):429-437.
APA Li, Z. X..,Zhang, X. Q..,Zhang, H. G..,Cao, S. H..,Wang, D. W..,...&Wang, X. P..(2008).Isolation and characterization of a novel variant of HMW glutenin subunit gene from the St genome of Pseudoroegneria stipifolia.JOURNAL OF CEREAL SCIENCE,47(3),429-437.
MLA Li, Z. X.,et al."Isolation and characterization of a novel variant of HMW glutenin subunit gene from the St genome of Pseudoroegneria stipifolia".JOURNAL OF CEREAL SCIENCE 47.3(2008):429-437.
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