ArticleThe journal of physical chemistry. B2013
Interaction of proteins associated with the magnetosome assembly in magnetotactic bacteria as revealed by two-hybrid two-photon excitation fluorescence lifetime imaging microscopy Förster resonance energy transfer.
Article in The journal of physical chemistry. B, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 30 citations in OpenAlex.
- Tumor-targeting inorganic nanomaterials synthesized by living cells.Nanoscale advances · 2021Review
- The in vivo mechanics of the magnetotactic backbone as revealed by correlative FLIM-FRET and STED microscopy.Scientific reports · 2019Article
- Tuning properties of biomimetic magnetic nanoparticles by combining magnetosome associated proteins.Scientific reports · 2019Article
- Segregation of prokaryotic magnetosomes organelles is driven by treadmilling of a dynamic actin-like MamK filament.BMC biology · 2016Article
- From invagination to navigation: The story of magnetosome-associated proteins in magnetotactic bacteria.Protein science : a publication of the Protein Society · 2016Review
- Bacterial protein networks: properties and functions.Nature reviews. Microbiology · 2015Review
- Biologically controlled synthesis and assembly of magnetite nanoparticles.Faraday discussions · 2015Article
- Probing the mechanical properties of magnetosome chains in living magnetotactic bacteria.Nano letters · 2014Article
- Structure prediction of magnetosome-associated proteins.Frontiers in microbiology · 2014Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria have recently revealed an unexpectedly complex level of intracellular organization. Magnetotactic bacteria represent a unique class of such organization through the presence of their magnetosome organelles, which are organized along the magnetosome filament. Although the role of individual magnetosomes-associated proteins has started to be unraveled, their interaction has not been addressed with current state-of-the-art optical microscopy techniques, effectively leaving models of the magnetotactic bacteria protein assembly arguable. Here we report on the use of FLIM-FRET to assess the interaction of MamK (actin-like protein) and MamJ, two magnetosome membrane associated proteins essential to the assembly of magnetosomes in a chain. We used a host organism (E. coli) to express eGFP_MamJ and MamK_mCherry, the latest expectedly forming a filament. We found that in the presence of MamK the fluorescence of eGFP_MamJ is distributed along the MamK filament. FRET analysis using the fluorescence lifetime of the donor, eGFP, revealed a spatial proximity of MamK_mCherry and eGFP_MamJ typical of a stable physical interaction between two proteins. Our study effectively led to the reconstruction of part of the magnetotactic apparatus in vivo.
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