Journal
FEBS OPEN BIO
Volume 3, Issue -, Pages 218-224Publisher
WILEY
DOI: 10.1016/j.fob.2013.04.004
Keywords
Circular dichroism spectroscopy; Histidine-rich loop; Isothermal titration calorimetry; Metal tolerance protein; Zinc binding; Zinc transporter
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Funding
- Japan Society for the Promotion of Science [23248017, 23657031]
- Salt Science Foundation [1223]
- Steel Foundation for Environmental Protection Technology [2010-29]
- JSPS
- Grants-in-Aid for Scientific Research [24114706, 23248017, 23657031] Funding Source: KAKEN
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The vacuolar Zn2+/H+ antiporter of Arabidopsis thaliana, AtMTP1, has a cytosolic histidine-rich loop (His-loop). We characterized the structures and Zn2+-binding properties of the His-loop and other domains. Circular dichroism analyses revealed that the His-loop partly consists of a polyproline type II structure and that its conformational change is induced by Zn2+ as well as the C-terminal domain. Isothermal titration calorimetry of the His-loop revealed a binding number of four Zn2+ per molecule. Numbers of Ni and Co associated with the His-loop were approximately one ion per molecule and the thermodynamic parameters of the association with these ions were different from that of Zn2+ These results suggest the involvement of the His-loop in sensing cytosolic Zn2+ and in the regulation of zinc transport activity through Zn2+-induced structural change. (C) 2013 The Authors. Published by Elsevier B.V. on behalf of Federation of European Biochemical Societies. All rights reserved.
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