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Revisiting the Potential Functionality of the MagR Protein

Authors :
Alexander Pekarsky
Herwig Michor
Oliver Spadiut
Source :
Magnetochemistry, Vol 7, Iss 11, p 147 (2021)
Publication Year :
2021
Publisher :
MDPI AG, 2021.

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.

Details

Language :
English
ISSN :
23127481
Volume :
7
Issue :
11
Database :
Directory of Open Access Journals
Journal :
Magnetochemistry
Publication Type :
Academic Journal
Accession number :
edsdoj.5cfd62c6942e48949112b5406aadfb16
Document Type :
article
Full Text :
https://doi.org/10.3390/magnetochemistry7110147