Possible role of iron containing proteins in physiological responses of soybean to static magnetic field
•Soybean differentially responded to 20 and 30 mT SMF through Fe-transporter, CAT, and Ferritin.•SMF did not change secondary structure but changed tertiary structure, size, and activity of CAT, ferritin and apoferritin.•Perception and response of the plants to magnetic field is mediated by iron-con...
Gespeichert in:
Veröffentlicht in: | Journal of plant physiology 2018-07, Vol.226, p.163-171 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
Zusammenfassung: | •Soybean differentially responded to 20 and 30 mT SMF through Fe-transporter, CAT, and Ferritin.•SMF did not change secondary structure but changed tertiary structure, size, and activity of CAT, ferritin and apoferritin.•Perception and response of the plants to magnetic field is mediated by iron-containing proteins.
Iron is a component of many proteins that have crucial roles in plant growth and development, such as ferritin and catalase. Iron also, as a ferromagnetic element, is assumed to be influenced by a static magnetic field (SMF). In the present study, we examined the relationship between ferrous content and gene expression and activity of ferritin and catalase in soybean plants under the influence of 0, 20, and 30 mT SMF for 5 day, 5 h each. Exposure to 20 mT decreased gene expression of Fe transporter, ferrous and H2O2 contents and gene expression, content and activity of ferritin and catalase. Opposite responses were observed under 30 mT treatments. The results suggest that SMF triggered a signaling pathway that is mediated by iron. The structure and activity of purified ferritin and apoferritin from horse spleen, and catalase from bovine liver proteins under SMF were evaluated as well. Secondary structure of proteins were not influenced by SMF (evidenced by far-UV circular dichroism), whereas their tertiary structure, size, and activity were altered (shown by fluorescence spectroscopy and dynamic light-scattering). From these results, it is likely that the number of iron atoms is involved in the nature of influence of SMF on protein structure. |
---|---|
ISSN: | 0176-1617 1618-1328 |
DOI: | 10.1016/j.jplph.2018.04.018 |