ArticleProtein science : a publication of the Protein Society2022
Magnetic field effects on the structure and molecular behavior of pigeon iron-sulfur protein.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Article
- Mitochondria as key targets underlying hypomagnetic field-induced biological effects.iScience · 2026Review
- Filamentous morphology engineering of bacteria by iron metabolism modulation through MagR expression.Synthetic and systems biotechnology · 2024Article
- Mitochondrial targeting sequence of magnetoreceptor MagR: More than just targeting.Zoological research · 2024Article
- Unexpected divergence in magnetoreceptor MagR from robin and pigeon linked to two sequence variations.Zoological research · 2024Article
- Towards magnetism in pigeon MagR: Iron- and iron-sulfur binding work indispensably and synergistically.Zoological research · 2023Article
- Magnetic field effects on the structure and molecular behavior of pigeon iron-sulfur protein.Protein science : a publication of the Protein Society · 2022Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pigeon iron-sulfur (Fe-S) cluster assembly 1 homolog (clISCA1) is a target protein for research into the biomagnetoreception mechanism, as the clCRY4/clISCA1 oligomer, a complex composed of the columnar clISCA1 oligomer and the magnetosensor candidate protein cryptochrome-4 (clCRY4) oligomer, tends to orient itself along weak magnetic fields, such as geomagnetic fields, under blue light. To obtain insight into the magnetic orientation mechanism of the clCRY4/clISCA1 oligomer, we inspected magnetic field effects on the structure and molecular behavior of clISCA1 by small angle X-ray scattering analysis. The results indicated that the clISCA1 protomer took the Fe-S cluster-bound globular form and unbound rod-like form. The globular clISCA1 protomer assembled to form columnar oligomers, which allowed for the binding of many Fe-S clusters at the interface between clISCA1 protomers. Moreover, the translational diffusion and the columnar oligomerization of clISCA1 were controlled by the external static magnetic field and Fe-S clusters bound to clISCA1. However, the columnar clISCA1 oligomer was not oriented along the external static magnetic field (~1 T) when clCRY4 was not bound to clISCA1. This result indicated that clCRY4 has a function to enhance the magnetic orientational property of clCRY4/clISCA1 oligomer.
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