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Updated: Apr 26, 2026

Growing Magnetotactic Bacteria of the Genus Magnetospirillum: Strains MSR-1, AMB-1 and MS-1
Published on: October 17, 2018
A magnetosome-associated cytochrome MamP is critical for magnetite crystal growth during the exponential growth phase
Azuma Taoka1, Yukako Eguchi, Shingo Mise
1School of Natural System, College of Science and Engineering, Kanazawa University, Kakuma-machi, Kanazawa, Japan; Bio-AFM Frontier Research Center, College of Science and Engineering, Kanazawa University, Kakuma-machi, Kanazawa, Japan.
Abstract:
Magnetotactic bacteria use a specific set of conserved proteins to biomineralize crystals of magnetite or greigite within their cells in organelles called magnetosomes. Using Magnetospirillum magneticum AMB-1, we examined one of the magnetotactic bacteria-specific conserved proteins named MamP that was recently reported as a new type of cytochrome c that has iron oxidase activity. We found that MamP is a membrane-bound cytochrome, and the MamP content increases during the exponential growth phase compared to two other magnetosome-associated proteins on the same operon, MamA and MamK. To assess the function of MamP, we overproduced MamP from plasmids in wild-type (WT) AMB-1 and found that during the exponential phase of growth, these cells contained more magnetite crystals that were the same size as crystals in WT cells. Conversely, when the heme c-binding motifs within the mamP on the plasmid was mutated, the cells produced the same number of crystals, but smaller crystals than in WT cells during exponential growth. These results strongly suggest that during the exponential phase of growth, MamP is crucial to the normal growth of magnetite crystals during biomineralization.
Insights
Magnetotactic bacteria use MamP protein for iron biomineralization. This membrane-bound cytochrome is crucial for normal magnetite crystal growth during bacterial exponential growth.
Area of Science:
- Microbiology
- Biochemistry
- Biomineralization
Background:
- Magnetotactic bacteria synthesize intracellular magnetic crystals (magnetite or greigite) within organelles called magnetosomes.
- These bacteria utilize a conserved set of proteins for this biomineralization process.
- MamP, a novel cytochrome c with iron oxidase activity, is one such magnetosome-associated protein.
Purpose of the Study:
- To investigate the function of the magnetotactic bacteria-specific protein MamP in magnetite biomineralization.
- To determine the role of MamP in the growth and size regulation of magnetite crystals in Magnetospirillum magneticum AMB-1.
Main Methods:
- Studied Magnetospirillum magneticum AMB-1, a model organism for magnetotactic bacteria.
- Quantified MamP protein levels during different growth phases.
- Overexpressed wild-type and mutated MamP (lacking heme c-binding motifs) in AMB-1 using plasmids.
- Analyzed the number and size of magnetite crystals in genetically modified and wild-type cells.
Main Results:
- MamP is a membrane-bound cytochrome whose expression increases during the exponential growth phase.
- Overexpression of MamP in wild-type AMB-1 led to an increased number of magnetite crystals of normal size.
- Mutating the heme c-binding motifs in MamP resulted in smaller magnetite crystals, despite normal crystal numbers.
Conclusions:
- MamP plays a critical role in regulating the normal growth and size of magnetite crystals during the exponential growth phase in magnetotactic bacteria.
- The iron oxidase activity of MamP is essential for proper magnetite biomineralization.
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