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

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 T 2 contrast agents for MRI application. We examined the ability of clMagR/clCry4 to mineralizing iron biominerals suitable for detection on MRI. The recombinant bacteria brings us closer to iron-mineralized cellular life. Prokaryotic E. coli , a microbial cell factory, was used as model organism and grown in rich iron exposed cultures at mineralize biominerals. It is hypothesized that that except for that clMagR/clCry4 have specifically been designed for iron biomineralization, clMagR and clCry4 are potentially involved in concerted processes. Accordingly, the formation of iron biominerals is a consequence of the associated proteins and exogenous iron co-contributed to mineralization. Going forward, inspiring mineralization by MagR/Cry4 could mean a big step forward in understanding the mechanism of magnetoreception. • This work provides the first report of clMagR/clCry4 deemed as a likely candidate as iron biomineralization protein. • As for clMagR/clCry4-mediated biomineralization, clMagR and clCry4 should not be ignored, nor the contributions ever perish. • Iron biomineralization by mediation of clMagR/clCry4 could give the clearer indications on a potential magnetoreception.

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Publication Details

Journal
Colloids and Interface Science Communications
Published
2024-12-04
DOI
https://doi.org/10.1016/j.colcom.2024.100810
Primary Topic
Geomagnetism and Paleomagnetism Studies
Type
article
Field-Weighted Citation Impact
0.00

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

Xiaoli Mai, Fangxu Wang, Linyuan Wu, Nuan Li et al.
Colloids and Interface Science Communications
Geomagnetism and Paleomagnetism Studies
article

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

Xiaoli Mai, Fangxu Wang, Linyuan Wu, Nuan Li, Peng Wang, Yuanyuan Xie, Bin Wang, Xiaofeng Han
article en

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 T 2 contrast agents for MRI application. We examined the ability of clMagR/clCry4 to mineralizing iron biominerals suitable for detection on MRI. The recombinant bacteria brings us closer to iron-mineralized cellular life. Prokaryotic E. coli , a microbial cell factory, was used as model organism and grown in rich iron exposed cultures at mineralize biominerals. It is hypothesized that that except for that clMagR/clCry4 have specifically been designed for iron biomineralization, clMagR and clCry4 are potentially involved in concerted processes. Accordingly, the formation of iron biominerals is a consequence of the associated proteins and exogenous iron co-contributed to mineralization. Going forward, inspiring mineralization by MagR/Cry4 could mean a big step forward in understanding the mechanism of magnetoreception. • This work provides the first report of clMagR/clCry4 deemed as a likely candidate as iron biomineralization protein. • As for clMagR/clCry4-mediated biomineralization, clMagR and clCry4 should not be ignored, nor the contributions ever perish. • Iron biomineralization by mediation of clMagR/clCry4 could give the clearer indications on a potential magnetoreception.

Colloids and Interface Science CommunicationsVol. 64
Nanjing Drum Tower Hospital (CN), Southeast University (CN)
Key Technologies Research and Development Program, National Key Research and Development Program of China
Zero hunger
Openalex Percentile: Top 81%
Geomagnetism and Paleomagnetism Studies
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