Iron biomineralization by mediation of clMagR/clCry4 protein contribute to T2 contrast enhanced in MRI

Abstract

Recent findings have sparked great interest in MagR/Cry4 protein that underpin animal magnetoreception. We tried to make progress in characterizing the Columba livia clMagR/clCry4, and connecting its properties to biological impacts. Throughout natural evolution, new functions of protein were never constructed from scratch, but from pre-existing parts. The clMagR/clCry4 was certainly not an exception. By employing synthetic biology, protein heterologous expression approach allowed protein function to be borrowed from nature to study their new traits. We introduced clMagR/clCry4 into the natural bacteria constructing the recombinant bacteria that perform biomineralization process. Our current work efforts were focused on investigating iron biomineralization in clMagR/clCry4 using electron microscopy. This is only one study, thus far, that describes clMagR/clCry4 deem as a likely candidate as iron biomineralization protein. Notably, iron biomineralization brings clMagR/clCry4 closer to its potential magnetoreception. Additionally, the obtained iron biominerals have shown a great promise to serve as T₂ contrast agents for MRI application.