Abstract
Recent findings have sparked great interest in the putative magnetic receptor protein MagR. However, in vivo experiments have revealed no magnetic moment of MagR at room temperature. Nevertheless, the interaction of MagR and MagR fusion proteins with silica-coated magnetite beads have proven useful for protein purification. In this study, we recombinantly produced two different MagR proteins in Escherichia coli BL21(DE3) to (1) expand earlier protein purification studies, (2) test if MagR can magnetize whole E. coli cells once it is expressed to a high cytosolic, soluble titer, and (3) investigate the MagR-expressing E. coli cells’ magnetic properties at low temperatures. Our results show that MagR induces no measurable, permanent magnetic moment in cells at low temperatures, indicating no usability for cell magnetization. Furthermore, we show the limited usability for magnetic bead-based protein purification, thus closing the current knowledge gap between theoretical considerations and empirical data on the MagR protein.
Highlights
Functionality of the magnetic receptor protein (MagR) Protein.Iron–sulfur (Fe–S) cluster proteins are important for numerous physiological processes and are present in most known prokaryotic and eukaryotic cells [1,2,3]
Binding studies with Drosophila melanogaster (dMagR)-his on SiO2 -Fe3 O4 beads showed that the protein was enriched from E. coli lysates
When we compared the efficiency of the magnetic bead capture with a state-of-the-art immobilized metal affinity chromatography (IMAC) capture, we found that the IMAC
Summary
Iron–sulfur (Fe–S) cluster proteins are important for numerous physiological processes and are present in most known prokaryotic and eukaryotic cells [1,2,3]. The Fe–S cluster protein MagR (magnetic receptor) came into spotlight [5]. The authors proposed a possible answer to the question on navigation of migratory animals. They reported that MagR, a small (~14 kDa) [2Fe–2S] protein from pigeons with homologs in numerous species, forms a ferrimagnetic, multimeric complex that responds to magnetic fields in vitro. MagR fusion proteins were successfully captured from a complex matrix [6,7]
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