Spatial localization of Mms6 during biomineralization of Fe3O4nanocrystals inMagnetospirillum magneticumAMB-1

Oestreicher, Zachery; Mumper, Eric; Gassman, Carol; Bazylinski, Dennis A.; Lower, Steven K.; Lower, Brian H.

doi:10.1557/jmr.2016.41

Cited by 5 publications

(7 citation statements)

References 36 publications

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“…Recent work by Oestreicher et al has shown the localization of Mms6 in the magnetosome during the crystal growth, wherein it was found to be in direct contact with the crystals indicating its signicance in their formation. 16 Using in situ liquid cell High Angle Annular Dark Field-Scanning Transmission Electron Microscopy (HAADF-STEM), Kashyap et al reported the surface localization of ferric ions on the negatively charged Mms6 micelles, which forms an amorphous precursor phase to iron oxide, upon slow addition of NaOH. Further, in the presence of Mms6, nucleation was observed only on the Mms6 micelle surface and not in the bulk.…”

Section: Introductionmentioning

confidence: 99%

“…In contrast, in vivo studies have shown that Mms6 is not involved in the nucleation, but only in the crystal growth. 16,17 The hydrophilic C-terminal domain of Mms6 plays a critical role in the formation of these particles. 9,11,18 m2Mms6, a synthetic C-terminal domain mutant of the wild type Mms6, does not template the formation of larger, uniform magnetite crystals.…”

Section: Introductionmentioning

confidence: 99%

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Protein patterns template arrays of magnetic nanoparticles

et al. 2016

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Protein patterns template arrays of magnetic nanoparticles

et al. 2016

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“…[ 50 ] We observed variability in the crystals, where some appear more similar to those produced by wild type, which is consistent with evidence that Mms6 is only localized to a subset of magnetosomes. [ 94 ]…”

Section: Resultsmentioning

confidence: 99%

“…This is consistent with the observations that similar species make the same crystal form and size and random mutagenesis changes the number of crystals per cell, but not their shape. [ 21,102 ] In addition, expression timing and checkpoint control during biogenesis has also been seen to be important [ 70,94 ] and magnetosome membrane proteins that control crystal nucleation and growth have interdependent and redundant functions. [ 30,45,51,103 ] Therefore, using one chasses to build different IONPs may require the mining of whole operons or MAIs, the balancing of multiple genes, control over membrane invagination, and temporal circuits for gene expression ordering.…”

Section: Discussionmentioning

confidence: 99%

Genetic Tuning of Iron Oxide Nanoparticle Size, Shape, and Surface Properties in Magnetospirillum magneticum

Furubayashi

Wallace

González

et al. 2020

Adv Funct Materials

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Different applications require iron oxide nanoparticles (IONPs) of varying size, shape, crystallinity, and surfaces that can be controlled through the synthesis reaction conditions. Under ambient conditions, Magnetospirillum magneticum AMB‐1 builds uniform Fe3O4 IONPs with shapes and crystal forms difficult to achieve with chemical synthesis. Genetic engineering can be used to change their properties, but there are few tools to fine‐tune expression over a wide range. To this end, ribosome binding sites, minimal constitutive promoters, and inducible systems (IPTG, aTc, and OC6) with large dynamic range are designed. These are used to control M. magneticum genes that affect IONP properties, including size (mamC), morphology (mms6), chain length (mamK), and surface coating (mamC fusions). These systems increase the fraction of IONPs that are less than 30 nm, produce rounded particles, and lead to the production of intracellular chains with 24 or more IONPs. In addition, the R5 peptide from diatoms is found to silica coat the surface of metal oxide nanoparticles (Fe, Ti, Ta, Hf) and can be genetically directed to the IONP surface. This work demonstrates the genetic control of IONP properties, but also highlights the robustness of the system, which complicates genetic engineering to produce radically different particles and structures.

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“…To purify magnetosomes and prepare cell soluble and membrane fractions of M. magneticum AMB-1 (ATCC 700264), the protocol described in [33] was followed. To clone mms13 (amb0951 in M. magneticum AMB-1; [22]), genomic DNA from M. magneticum AMB-1 was obtained from the American Type Culture Collection (ATCC #700264).…”

Section: Methodsmentioning

confidence: 99%

Localization of Native Mms13 to the Magnetosome Chain of Magnetospirillum magneticum AMB-1 Using Immunogold Electron Microscopy, Immunofluorescence Microscopy and Biochemical Analysis

et al. 2021

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Magnetotactic bacteria (MTB) biomineralize intracellular magnetite (Fe3O4) crystals surrounded by a magnetosome membrane (MM). The MM contains membrane-specific proteins that control Fe3O4 mineralization in MTB. Previous studies have demonstrated that Mms13 is a critical protein within the MM. Mms13 can be isolated from the MM fraction of Magnetospirillum magneticum AMB-1 and a Mms13 homolog, MamC, has been shown to control the size and shape of magnetite nanocrystals synthesized in-vitro. The objective of this study was to use several independent methods to definitively determine the localization of native Mms13 in M. magneticum AMB-1. Using Mms13-immunogold labeling and transmission electron microscopy (TEM), we found that Mms13 is localized to the magnetosome chain of M. magneticum AMB-1 cells. Mms13 was detected in direct contact with magnetite crystals or within the MM. Immunofluorescence detection of Mms13 in M. magneticum AMB-1 cells by confocal laser scanning microscopy (CLSM) showed Mms13 localization along the length of the magnetosome chain. Proteins contained within the MM were resolved by SDS-PAGE for Western blot analysis and LC-MS/MS (liquid chromatography with tandem mass spectrometry) protein sequencing. Using Anti-Mms13 antibody, a protein band with a molecular mass of ~14 kDa was detected in the MM fraction only. This polypeptide was digested with trypsin, sequenced by LC-MS/MS and identified as magnetosome protein Mms13. Peptides corresponding to the protein’s putative MM domain and catalytic domain were both identified by LC-MS/MS. Our results (Immunogold TEM, Immunofluorescence CLSM, Western blot, LC-MS/MS), combined with results from previous studies, demonstrate that Mms13 and homolog proteins MamC and Mam12, are localized to the magnetosome chain in MTB belonging to the class Alphaproteobacteria. Because of their shared localization in the MM and highly conserved amino acid sequences, it is likely that MamC, Mam12, and Mms13 share similar roles in the biomineralization of Fe3O4 nanocrystals.

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Spatial localization of Mms6 during biomineralization of Fe₃O₄nanocrystals inMagnetospirillum magneticumAMB-1

Abstract: Abstract

Cited by 5 publications

References 36 publications

Protein patterns template arrays of magnetic nanoparticles

Protein patterns template arrays of magnetic nanoparticles

Genetic Tuning of Iron Oxide Nanoparticle Size, Shape, and Surface Properties in Magnetospirillum magneticum

Localization of Native Mms13 to the Magnetosome Chain of Magnetospirillum magneticum AMB-1 Using Immunogold Electron Microscopy, Immunofluorescence Microscopy and Biochemical Analysis

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