Structural element responsible for the Fe(III)-phytosiderophore specific transport by HvYS1 transporter in barley

被引:40
作者
Harada, Emiko [1 ]
Sugase, Kenji [1 ]
Namba, Kosuke [1 ]
Iwashita, Takashi [1 ]
Murata, Yoshiko [1 ]
机构
[1] Suntory Inst Bioorgan Res, Shimamoto, Osaka 6188503, Japan
来源
FEBS LETTERS | 2007年 / 581卷 / 22期
关键词
chimera; alpha-helix; iron acquisition; iron-phytosiderophore; substrate specificity; transporter;
D O I
10.1016/j.febslet.2007.08.011
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Hordeum vulgare L. yellow stripe 1 (HvYS1) is a selective transporter for Fe(Ill)-phytosiderophores, involved in primary iron acquisition from soils in barley roots. In contrast, Zea mays yellow stripe 1 (ZmYS1) in maize possesses broad substrate specificity, despite a high homology with HvYS1. Here we revealed, by assessing the transport activity of a series of HvYS1-ZmYS1 chimeras, that the outer membrane loop between the sixth and seventh transmembrane regions is essential for substrate specificity. Circular dichroism spectra indicated that a synthetic peptide corresponding to the loop of HvYS1 forms an a-helix in solution, whereas that of ZmYS1 is flexible. We propose that the structural difference at this particular loop determines the substrate specificity of the HvYS1 transporter. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:4298 / 4302
页数:5
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