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magnetochemistryArticleRevisiting the Prospective Functionality of your MagR ProteinAlexander Pekarsky 1 , Herwig Michorand Oliver Spadiut 1, Institute of Chemical, Environmental and Bioscience Engineering, Study Location Biochemical Engineering, TU Wien, 1060 Wien, Austria; [email protected] Institute of Solid State Physics, TU Wien, 1040 Wien, Austria; [email protected] Correspondence: [email protected]: Current findings have sparked terrific interest inside the putative magnetic receptor protein MagR. Even so, 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 confirmed helpful 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, (two) test if MagR can magnetize complete E. coli cells after it’s 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. In addition, we show the limited usability for magnetic bead-based protein purification, as a Seclidemstat Epigenetics result closing the present understanding gap in between theoretical considerations and empirical information on the MagR protein. Key phrases: magnetic receptor protein (MagR); Escherichia coli; magnetism; affinity chromatography; SQUIDCitation: Pekarsky, A.; Michor, H.; Spadiut, O. Revisiting the Possible Functionality with the MagR Protein. Magnetochemistry 2021, 7, 147. https://doi.org/10.3390/ magnetochemistry7110147 Academic Editor: Kevin Bernot Received: 20 October 2021 Accepted: 9 November 2021 Published: 11 November1. Introduction Iron ulfur (Fe ) cluster proteins are important for several physiological processes and are present in most known prokaryotic and eukaryotic cells [1]. The iron atoms in [2FeS] clusters have already been reported to interact via antiferromagnetic coupling [4]. Only not too long ago, the Fe cluster protein MagR (magnetic receptor) came into spotlight [5]. The authors proposed a doable ML-SA1 Epigenetic Reader Domain answer towards the question on navigation of migratory animals. They reported that MagR, a tiny ( 14 kDa) [2FeS] protein from pigeons with homologs in numerous species, forms a ferrimagnetic, multimeric complicated that responds to magnetic fields in vitro. Qin et al. also showed that the MagR protein and a MagR/Cryptochrome complex may be isolated and enriched from a complicated matrix by silica-coated magnetite (SiO2 e3 O4 ) beads [5]. Later, MagR fusion proteins had been effectively captured from a complex matrix [6,7]. Considering the fact that its discovery, the physical capabilities of MagR have already been intensively questioned. When MagR constructs had been subjected to magnetic stimuli in mammalian cells, they weren’t able to induce substantial membrane channel activity within a magnetic field [8], in contrast to earlier benefits [9]. The biologist Markus Me.
