The helical propensity of the extracellular loop is responsible for the substrate specificity of Fe(III)-phytosiderophore transporters

• Harada, Erisa

• Sugase, Kenji

• Namba, Kosuke

• Murata, Yoshiko

Bibliographic Information

Other Title

• Specificity of iron-phytosiderophore transporter

Abstract

Hordeum vulgare L. yellow stripe 1 (HvYS1) is a selective transporter of Fe(III)-phytosiderophores in barley that is responsible for iron acquisition from the soil. In contrast, maize Zea mays, yellow stripe 1 (ZmYS1) possesses broad substrate specificity. In this study, a quantitative evaluation of the transport activities of HvYS1 and ZmYS1 chimera proteins revealed that the seventh extracellular membrane loop is essential for substrate specificity. The loop peptides of both transporters were prepared and analysed by circular dichroism and NMR. The spectra revealed a higher propensity for α-helical conformation of the HvYS1 loop peptide and a largely disordered structure for that of ZmYS1. These structural differences are potentially responsible for the substrate specificities of the transporters.

Journal

• FEBS Letters

  FEBS Letters 590 (24), 4617-4627, 2016-11-11

  Federation of European Biochemical Societies|Wiley

Keywords

• α-helical content
• phytosiderophore
• YS1 transporter

Details

• CRID: 1050006144166667264
• NII Article ID: 120006939615
• NII Book ID: AA00642943
• ISSN: 18733468
• Web Site: http://repo.lib.tokushima-u.ac.jp/114563
• Text Lang: en
• Article Type: journal article
• Data Source:
  • IRDB
  • CiNii Articles