Revisiting the Potential Functionality of the MagR Protein
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...
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MDPI AG
2021-11-01
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Series: | Magnetochemistry |
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Online Access: | https://www.mdpi.com/2312-7481/7/11/147 |
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author | Alexander Pekarsky Herwig Michor Oliver Spadiut |
author_facet | Alexander Pekarsky Herwig Michor Oliver Spadiut |
author_sort | Alexander Pekarsky |
collection | DOAJ |
description | 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 <i>Escherichia coli</i> BL21(DE3) to (1) expand earlier protein purification studies, (2) test if MagR can magnetize whole <i>E. coli</i> cells once it is expressed to a high cytosolic, soluble titer, and (3) investigate the MagR-expressing <i>E. coli</i> 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. |
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format | Article |
id | doaj.art-5cfd62c6942e48949112b5406aadfb16 |
institution | Directory Open Access Journal |
issn | 2312-7481 |
language | English |
last_indexed | 2024-03-10T05:19:42Z |
publishDate | 2021-11-01 |
publisher | MDPI AG |
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series | Magnetochemistry |
spelling | doaj.art-5cfd62c6942e48949112b5406aadfb162023-11-23T00:06:45ZengMDPI AGMagnetochemistry2312-74812021-11-0171114710.3390/magnetochemistry7110147Revisiting the Potential Functionality of the MagR ProteinAlexander Pekarsky0Herwig Michor1Oliver Spadiut2Institute of Chemical, Environmental and Bioscience Engineering, Research Area Biochemical Engineering, TU Wien, 1060 Wien, AustriaInstitute of Solid State Physics, TU Wien, 1040 Wien, AustriaInstitute of Chemical, Environmental and Bioscience Engineering, Research Area Biochemical Engineering, TU Wien, 1060 Wien, AustriaRecent 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 <i>Escherichia coli</i> BL21(DE3) to (1) expand earlier protein purification studies, (2) test if MagR can magnetize whole <i>E. coli</i> cells once it is expressed to a high cytosolic, soluble titer, and (3) investigate the MagR-expressing <i>E. coli</i> 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.https://www.mdpi.com/2312-7481/7/11/147magnetic receptor protein (MagR)<i>Escherichia coli</i>magnetismaffinity chromatographySQUID |
spellingShingle | Alexander Pekarsky Herwig Michor Oliver Spadiut Revisiting the Potential Functionality of the MagR Protein Magnetochemistry magnetic receptor protein (MagR) <i>Escherichia coli</i> magnetism affinity chromatography SQUID |
title | Revisiting the Potential Functionality of the MagR Protein |
title_full | Revisiting the Potential Functionality of the MagR Protein |
title_fullStr | Revisiting the Potential Functionality of the MagR Protein |
title_full_unstemmed | Revisiting the Potential Functionality of the MagR Protein |
title_short | Revisiting the Potential Functionality of the MagR Protein |
title_sort | revisiting the potential functionality of the magr protein |
topic | magnetic receptor protein (MagR) <i>Escherichia coli</i> magnetism affinity chromatography SQUID |
url | https://www.mdpi.com/2312-7481/7/11/147 |
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